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evolution
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acetyltransferases are very well conserved through evolution
evolution
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acetyltransferases are very well conserved through evolution
evolution
histone acetyltransferase KAT8 is a member of the MYST family
evolution
histone acetyltransferase p300 is a member of the p300/CBP family
evolution
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histone acetyltransferase p300/CBP-associated factor (PCAF) belongs to GCN5 family
evolution
tehe enzyme belongs to the p300/CBP enzyme family
evolution
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the Arabidopsis genome contains 12 histone acetyltransferase genes
evolution
the enzyme belongs to the GCN5-family of lysine acetyltransferases
evolution
the enzyme belongs to the MYST family
evolution
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Tip60, the 60 kDa HIV-1 Tat-interactive protein, is a key member of the MYST family of histone acetyltransferases (HATs)
evolution
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according to the allosteric ligand type of the ACT domain, members of AAPatA family are divided into two groups, the asparagine (Asn)-activated PatA and the cysteine (Cys)-activated PatA. The former exists only in Streptomyces, the latter are distributed in other actinobacteria (Pseudonocardiaceae, Micromonosporaceae, Nocardiopsaceae, and Streptosporangiaceae)
evolution
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according to the allosteric ligand type of the ACT domain, members of AAPatA family are divided into two groups, the asparagine (Asn)-activated PatA and the cysteine (Cys)-activated PatA. The former exists only in Streptomyces, the latter are distributed in other actinobacteria (Pseudonocardiaceae, Micromonosporaceae, Nocardiopsaceae, and Streptosporangiaceae)
evolution
HBO1 (also known as KAT7, MYST2) is a canonical member of the MYST (MOZ, Ybf1/Sas3, Sas2 and Tip60) acetyltransferase family. HBO1 contains the MYST domain that is a highly conserved acetyltransferase domain shared by the MYST family such as MYST1 (MOF/KAT8), MYST2 (HBO1/KAT7), and MYST3 (MOZ/KAT6A). HBO1 comprises a cervical-loop structure proximity to the MYST domain that mediates the interaction with the N-terminal region (residues 31-80) of BRPF2 (also known as BRD1), for BRPF2 is a cofactor directing HBO1 binding to the histone
evolution
HBO1 (also known as KAT7, MYST2) is a canonical member of the MYST (MOZ, Ybf1/Sas3, Sas2 and Tip60) acetyltransferase family. HBO1 contains the MYST domain that is a highly conserved acetyltransferase domain shared by the MYST family such as MYST1 (MOF/KAT8), MYST2 (HBO1/KAT7), and MYST3 (MOZ/KAT6A). HBO1 comprises a cervical-loop structure proximity to the MYST domain that mediates the interaction with the N-terminal region (residues 31-80) of BRPF2 (also known as BRD1), for BRPF2 is a cofactor directing HBO1 binding to the histone
evolution
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 the enzyme belongs to the components of transcription factor complexes
evolution
the enzyme belongs to the GCN5-related N-acetyltransferase (GNAT) superfamily. The GNAT superfamily of proteins is involved in many physiologically important reactions in eukaryotes and prokaryotes. PA4534 shares common characteristic structures with other GNAT family N-acetyltransferases and contains a potential substrate binding tunnel close to the bound acetyl-CoA. It also shows the characteristic features of GNAT proteins including the beta-bulge in b4 and the P-loop between beta4 and alpha3. The P-loop of PA4534 locates between beta4 and alpha3 that connects the diphosphate group of acetyl-CoA with the main chain nitrogen atoms from residues including G81, G83, A85, and R86
evolution
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 the enzyme belongs to the MYST family. The MYST family takes its name from the first identified members: (MOZ, KAT6A), Ybf2 (Sas3, KAT6), something about silencing (Sas2, KAT8) and Tat-interacting protein (Tip60, KAT5). To date, five human KATs have been identified in this family: MOZ, MOZ related factor (MORF, KAT6B), Tip60, HAT bound to ORC1 (HBO1, KAT7) and males absent on the first (MOF, KAT8 or MYST 1), the functional orthologue of yeast's Sas2. The defining feature of MYST family is the presence of the highly conserved MYST domain. MYST enzymes possess a highly-conserved acetyl-CoA-binding motif A within the catalytic domain. Additionally, some family members have also structural features in common with one another, such as chromodomains or plant homeodomain-linked zinc fingers. The members of this family utilize a double displacement (or ping-pong) catalytic mechanism. Autoacetylation is an important process in modulating the activity of MYST family members
evolution
the enzyme belongs to the MYST family. The MYST family takes its name from the first identified members: (MOZ, KAT6A), Ybf2 (Sas3, KAT6), something about silencing (Sas2, KAT8) and Tat-interacting protein (Tip60, KAT5). To date, five human KATs have been identified in this family: MOZ, MOZ related factor (MORF, KAT6B), Tip60, HAT bound to ORC1 (HBO1, KAT7) and males absent on the first (MOF, KAT8 or MYST 1), the functional orthologue of yeast's Sas2. The defining feature of MYST family is the presence of the highly conserved MYST domain. MYST enzymes possess a highly-conserved acetyl-CoA-binding motif A within the catalytic domain. Additionally, some family members have also structural features in common with one another, such as chromodomains or plant homeodomain-linked zinc fingers. The members of this family utilize a double displacement (or ping-pong) catalytic mechanism. Autoacetylation is an important process in modulating the activity of MYST family members
evolution
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 the enzyme belongs to the nuclear receptors coactivators
evolution
the enzyme belongs to the nuclear receptors coactivators. Fungal enzyme Rtt109 shows low sequence similarity to members of other KAT families. It is comparable to p300 in terms of its tertiary structure, but has a different catalytic mechanism
evolution
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 the enzyme TAF1/TBP belongs to the components of transcription factor complexes
evolution
the enzyme TAF1/TBP belongs to the components of transcription factor complexes
evolution
the enzyme TAF1/TBP belongs to the components of transcription factor complexes
evolution
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 the KATs belong to the enzyme families Gcn5 (KAT2A), PCAF (p300/CBP associated factor, KAT2B), Elp3 (KAT9), Hpa2 (KAT10), Hpa3, and Nut1. The common feature is the presence of four conserved 15-33 amino acid motifs indicated as A, B, C and D, in addition to various chromo- and bromodomains that can bind methylated or acetylated lysines, respectively. The A motif is the most conserved and contains the R/Q-X-X-G-X-G/A sequence that is essential for acetyl-CoA recognition and binding. Despite the structural similarities that characterize an enzyme family, the N- and C-terminal domains are quite different, and allow each enzyme to be specific for a particular substrate
evolution
the KATs belong to the enzyme families Gcn5 (KAT2A), PCAF (p300/CBP associated factor, KAT2B), Elp3 (KAT9), Hpa2 (KAT10), Hpa3, and Nut1. The common feature is the presence of four conserved 15-33 amino acid motifs indicated as A, B, C and D, in addition to various chromo- and bromodomains that can bind methylated or acetylated lysines, respectively. The A motif is the most conserved and contains the R/Q-X-X-G-X-G/A sequence that is essential for acetyl-CoA recognition and binding. Despite the structural similarities that characterize an enzyme family, the N- and C-terminal domains are quite different, and allow each enzyme to be specific for a particular substrate
evolution
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 the KATs belong to the enzyme families Gcn5 (KAT2A), PCAF (p300/CBP associated factor, KAT2B), Elp3 (KAT9), Hpa2 (KAT10), Hpa3, and Nut1. The common feature is the presence of four conserved 15-33 amino acid motifs indicated as A, B, C and D, in addition to various chromo- and bromodomains that can bind methylated or acetylated lysines, respectively. The A motif is the most conserved and contains the R/Q-X-X-G-X-G/A sequence that is essential for acetyl-CoA recognition and binding. Despite the structural similarities that characterize an enzyme family, the N- and C-terminal domains are quite different, and allow each enzyme to be specific for a particular substrate. A characterizing feature of p300/CBP family is the presence of a loop, called the L1 loop, which connects an alpha-helix (alpha4) and a beta-sheet (beta5), and is part of the lysine and acetyl-CoA binding site
evolution
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 the KATs belong to the enzyme families Gcn5 (KAT2A), PCAF (p300/CBP associated factor, KAT2B), Elp3 (KAT9), Hpa2 (KAT10), Hpa3, and Nut1. The common feature is the presence of four conserved 15-33 amino acid motifs indicated as A, B, C and D, in addition to various chromo- and bromodomains that can bind methylated or acetylated lysines, respectively. The A motif is the most conserved and contains the R/Q-X-X-G-X-G/A sequence that is essential for acetyl-CoA recognition and binding. Despite the structural similarities that characterize an enzyme family, the N- and C-terminal domains are quite different, and allow each enzyme to be specific for a particular substrate. A characterizing feature of p300/CBP family is the presence of a loop, called the L1 loop, which connects an alpha-helix (alpha4) and a beta-sheet (beta5), and is part of the lysine and acetyl-CoA binding site. Enzyme CBP is implicated in Rubinstein-Taybi syndrome and inflammation and mutated in lung, colon and ovarian carcinomas. The enzyme forms fusion proteins in acute myeloid leukemia
evolution
there are three major families of KATs grouped according to their sequence homology and domain organizations, which include the MYST family, GCN5/PCAF family, and p300/CBP family
evolution
three main histone/protein acetyltransferase (HAT) families, CBP/p300, GNAT (GCN5/PCAF) and MYST exist. GCN5 belongs to the GNAT family
evolution
three main histone/protein acetyltransferase (HAT) families, CBP/p300, GNAT (GCN5/PCAF) and MYST exist. PCAF belongs to the GNAT family
evolution
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the enzyme belongs to the GCN5-related N-acetyltransferase (GNAT) superfamily. The GNAT superfamily of proteins is involved in many physiologically important reactions in eukaryotes and prokaryotes. PA4534 shares common characteristic structures with other GNAT family N-acetyltransferases and contains a potential substrate binding tunnel close to the bound acetyl-CoA. It also shows the characteristic features of GNAT proteins including the beta-bulge in b4 and the P-loop between beta4 and alpha3. The P-loop of PA4534 locates between beta4 and alpha3 that connects the diphosphate group of acetyl-CoA with the main chain nitrogen atoms from residues including G81, G83, A85, and R86
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evolution
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according to the allosteric ligand type of the ACT domain, members of AAPatA family are divided into two groups, the asparagine (Asn)-activated PatA and the cysteine (Cys)-activated PatA. The former exists only in Streptomyces, the latter are distributed in other actinobacteria (Pseudonocardiaceae, Micromonosporaceae, Nocardiopsaceae, and Streptosporangiaceae)
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evolution
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the enzyme belongs to the GCN5-related N-acetyltransferase (GNAT) superfamily. The GNAT superfamily of proteins is involved in many physiologically important reactions in eukaryotes and prokaryotes. PA4534 shares common characteristic structures with other GNAT family N-acetyltransferases and contains a potential substrate binding tunnel close to the bound acetyl-CoA. It also shows the characteristic features of GNAT proteins including the beta-bulge in b4 and the P-loop between beta4 and alpha3. The P-loop of PA4534 locates between beta4 and alpha3 that connects the diphosphate group of acetyl-CoA with the main chain nitrogen atoms from residues including G81, G83, A85, and R86
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evolution
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the enzyme belongs to the GCN5-related N-acetyltransferase (GNAT) superfamily. The GNAT superfamily of proteins is involved in many physiologically important reactions in eukaryotes and prokaryotes. PA4534 shares common characteristic structures with other GNAT family N-acetyltransferases and contains a potential substrate binding tunnel close to the bound acetyl-CoA. It also shows the characteristic features of GNAT proteins including the beta-bulge in b4 and the P-loop between beta4 and alpha3. The P-loop of PA4534 locates between beta4 and alpha3 that connects the diphosphate group of acetyl-CoA with the main chain nitrogen atoms from residues including G81, G83, A85, and R86
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evolution
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the enzyme belongs to the GCN5-related N-acetyltransferase (GNAT) superfamily. The GNAT superfamily of proteins is involved in many physiologically important reactions in eukaryotes and prokaryotes. PA4534 shares common characteristic structures with other GNAT family N-acetyltransferases and contains a potential substrate binding tunnel close to the bound acetyl-CoA. It also shows the characteristic features of GNAT proteins including the beta-bulge in b4 and the P-loop between beta4 and alpha3. The P-loop of PA4534 locates between beta4 and alpha3 that connects the diphosphate group of acetyl-CoA with the main chain nitrogen atoms from residues including G81, G83, A85, and R86
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evolution
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the enzyme belongs to the GCN5-related N-acetyltransferase (GNAT) superfamily. The GNAT superfamily of proteins is involved in many physiologically important reactions in eukaryotes and prokaryotes. PA4534 shares common characteristic structures with other GNAT family N-acetyltransferases and contains a potential substrate binding tunnel close to the bound acetyl-CoA. It also shows the characteristic features of GNAT proteins including the beta-bulge in b4 and the P-loop between beta4 and alpha3. The P-loop of PA4534 locates between beta4 and alpha3 that connects the diphosphate group of acetyl-CoA with the main chain nitrogen atoms from residues including G81, G83, A85, and R86
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evolution
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the enzyme belongs to the GCN5-related N-acetyltransferase (GNAT) superfamily. The GNAT superfamily of proteins is involved in many physiologically important reactions in eukaryotes and prokaryotes. PA4534 shares common characteristic structures with other GNAT family N-acetyltransferases and contains a potential substrate binding tunnel close to the bound acetyl-CoA. It also shows the characteristic features of GNAT proteins including the beta-bulge in b4 and the P-loop between beta4 and alpha3. The P-loop of PA4534 locates between beta4 and alpha3 that connects the diphosphate group of acetyl-CoA with the main chain nitrogen atoms from residues including G81, G83, A85, and R86
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evolution
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the KATs belong to the enzyme families Gcn5 (KAT2A), PCAF (p300/CBP associated factor, KAT2B), Elp3 (KAT9), Hpa2 (KAT10), Hpa3, and Nut1. The common feature is the presence of four conserved 15-33 amino acid motifs indicated as A, B, C and D, in addition to various chromo- and bromodomains that can bind methylated or acetylated lysines, respectively. The A motif is the most conserved and contains the R/Q-X-X-G-X-G/A sequence that is essential for acetyl-CoA recognition and binding. Despite the structural similarities that characterize an enzyme family, the N- and C-terminal domains are quite different, and allow each enzyme to be specific for a particular substrate
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evolution
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the enzyme TAF1/TBP belongs to the components of transcription factor complexes
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evolution
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the enzyme belongs to the nuclear receptors coactivators. Fungal enzyme Rtt109 shows low sequence similarity to members of other KAT families. It is comparable to p300 in terms of its tertiary structure, but has a different catalytic mechanism
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evolution
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according to the allosteric ligand type of the ACT domain, members of AAPatA family are divided into two groups, the asparagine (Asn)-activated PatA and the cysteine (Cys)-activated PatA. The former exists only in Streptomyces, the latter are distributed in other actinobacteria (Pseudonocardiaceae, Micromonosporaceae, Nocardiopsaceae, and Streptosporangiaceae)
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evolution
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the enzyme belongs to the GCN5-related N-acetyltransferase (GNAT) superfamily. The GNAT superfamily of proteins is involved in many physiologically important reactions in eukaryotes and prokaryotes. PA4534 shares common characteristic structures with other GNAT family N-acetyltransferases and contains a potential substrate binding tunnel close to the bound acetyl-CoA. It also shows the characteristic features of GNAT proteins including the beta-bulge in b4 and the P-loop between beta4 and alpha3. The P-loop of PA4534 locates between beta4 and alpha3 that connects the diphosphate group of acetyl-CoA with the main chain nitrogen atoms from residues including G81, G83, A85, and R86
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malfunction
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cells lacking RTT109 have a high level of CAG/CTG repeat contractions and a twofold increase in breakage at CAG/CTG repeats
malfunction
disturbance of normal acetylation of K16 in histone H4 together with trimethylation of Lys20 in histone H4 is associated with early stages of tumor development
malfunction
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dysfunction is associated with diseases like asthma, cardiovascular disorders, diabetes, and cancer
malfunction
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dysfunction is associated with diseases like asthma, cardiovascular disorders, diabetes, and cancer
malfunction
dysfunction of histone acetyltransferases leads to several diseases including cancer, diabetes, and asthma
malfunction
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H4K16 hyperacetylation is associated with hyperexpression of the single male X chromosome in flies and, contrasting accordingly, the inactivated X chromosome in human cells is hypoacetylated at the same histone residue. HBO1 appears to function predominantly in transcriptional repression
malfunction
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HBO1 depletion reduces the rate of DNA synthesis, the amount of MCM complex bound to chromatin, and progression through S phase
malfunction
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MOZ generates fusion genes, such as MOZ-TIF2, MOZ-CBP and MOZ-p300, in acute myeloid leukemia by chromosomal translocation leading to repressed differentiation, hyper-proliferation, and self-renewal of myeloid progenitors through deregulation of MOZ-regulated target gene expression. Roles of MOZ and MOZ fusion genes in normal and malignant hematopoiesis, mechanism, overview
malfunction
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the haploinsufficient enzyme causes the Rubinstein-Taybi syndrome, a genetic disorder with cognitive dysfunction, by disrupting the control mechanism of neural precursor competency to differentiate
malfunction
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expression of mutant TgMYST-B produces no growth defect and fails to protect against DNA damage
malfunction
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overexpression of recombinant, tagged TgMYST-B reduces growth rate in vitro and confers protection from a DNA-alkylating agent. Cells overexpressing TgMYST-B have increased levels of ataxia telangiectasia mutated (ATM) kinase and phosphorylated H2AX and that TgMYST-B localizes to the ATM kinase gene. Pharmacological inhibitors of ATM kinase or KATs reverse the slow growth phenotype seen in parasites overexpressing TgMYST-B
malfunction
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aberrant histone acetylation contributes to disease
malfunction
antagonizing H4K16ac downregulation upon autophagy induction results in the promotion of cell death
malfunction
both histone H3 and H4 acetylation were increased upon GCN5 overexpression and decreased upon GCN5 knockdown
malfunction
enzyme inhibition significantly augments TRAIL-induced apoptotic sensitivity, which is accompanied by reduced levels of survivin, in Hep-G2, HLE and SK-HEP1 cells. Enzyme inhibition significantly decreases invasion of Huh7, HLE and SK-HEP1 cells. The level of matrix metallopeptidase 15 (MMP15) mRNA expression is significantly reduced, whereas the level of laminin alpha 3 (LAMA3) and secreted phosphoprotein 1 (SPP1) mRNA expression is significantly increased in Huh7 cells following exposure to enzyme inhibitor C646
malfunction
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enzyme PCAF-deficiency causes drastic decrease in mRNA levels of Bcl-6 and Pax5, and remarkable increase in that of B lymphocyte-induced maturation protein-1 (Blimp-1). In addition, PCAF-deficiency causes a remarkable decrease in acetylation levels of both H3K9 and H3K14 residues within chromatin surrounding the 5'-flanking regions of Bcl-6 and Pax5 genes in vivo
malfunction
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forced expression of PCAF inhibits the growth of hepatocellular carcinoma xenografts, upregulates histone H4 acetylation, suppresses phosphorylation of AKT, and accelerates cell apoptosis. Knockdown of PCAF represses cell apoptosis and accelerates proliferation in Hep-3B cells. Enzyme downregulation in hepatocellular carcinoma tissues is significantly correlated with tumor TNM staging and intrahepatic metastasis
malfunction
induced accumulation of the ddHAGCN5b(E703G) protein leads to a rapid arrest in parasite replication. Growth arrest is accompanied by a decrease in histone H3 acetylation at specific lysine residues as well as reduced expression of GCN5b target genes in GCN5b(E703G) parasites, which are identified using chromatin immunoprecipitation coupled with microarray hybridization
malfunction
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knockdown of GCN5 inhibits the osteogenic differentiation of and mineralization in mesenchymal stem cells. Impaired osteogenic differentiation by GCN5 knockdown is blocked by inhibition of NF-kappaB
malfunction
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loss of function of the Arabidopsis histone acetyltransferase GCN5 results in serious defects in terms of thermotolerance, and considerably impairs the transcriptional activation of heat stress-responsive genes. The expression of several key regulators such as the heat stress transcription factors HSFA2 and HSFA3, multiprotein bridging factor 1c (MBF1c) and UV-hypersensitive 6 (UVH6) is downregulated in the gcn5 mutant under heat stress compared with the wild-type. The GCN5 mutation affects H3K9 and H3K14 acetylation of HSFA3 and UVH6 genes under heat stress. Overexpression of the Triticum aestivum TaGCN5 gene restores thermotolerance in Arabidopsis gcn5 mutant plants
malfunction
PCAF deficiency reduces the in vitro inflammatory response in leukocytes and vascular cells involved in arteriogenesis. PCAF deficiency results in differential expression of 3505 genes during arteriogenesis and, more specifically, in impaired induction of multiple proinflammatory genes. Recruitment from the bone marrow of inflammatory cells, in particular proinflammatory Ly6Chi monocytes, is severely impaired in PCAF-/- mice
malfunction
small cell lung cancer cells are deficient of the histone acetyltransferase KAT6B. The depletion of KAT6B expression enhances cancer growth, while its restoration induces tumor suppressor-like features. Enzyme deletion or inhibition confers sensitivity to irinotecan, causes diminished expression of Brahma, and induces an increase in Rb phosphorylation
malfunction
the dysregulated gene expression induced by garcinol inhibition of the enzyme significantly inhibits Toxoplasma tachyzoite replication without being toxic to the human host cell. Garcinol inhibits TgGCN5b KAT activity and reduces global lysine acetylation in vivo in treated parasites, including its preferred substrate, histone H3
malfunction
abrogation of HBO1 activity caused by either RNA interference or dominant negative mutation (e.g. S57A) does not affect the recruitment of ORC, CDC6 and CDT1 to replication origins, but remarkably impairs the loading of MCMs to the origins and subsequently delays DNA replication licensing. In immune-related disease, HBO1 is upregulated in synovial fibroblasts, which are the key pathogenic factors contributing to the development and progression of rheumatoid arthritis. Protein HBZ (HTLV-1 basic zipper factor, from a human T cell leukemia virus) interacts with HBO1 during pathogenesis and inhibits its acetylation activity to reduce p53-mediated transcription activation of p21/CDKN1A and Gadd45a, and subsequently delays G2-cell cycle arrest
malfunction
abrogation of HBO1 activity caused by either RNA interference or dominant negative mutation (e.g. S57A) does not affect the recruitment of ORC, CDC6 and CDT1 to replication origins, but remarkably impairs the loading of MCMs to the origins and subsequently delays DNA replication licensing. In immune-related disease, HBO1 is upregulated in synovial fibroblasts, which are the key pathogenic factors contributing to the development and progression of rheumatoid arthritis. Protein HBZ (HTLV-1 basic zipper factor, from a human T cell leukemia virus) interacts with HBO1 during pathogenesis and inhibits its acetylation activity to reduce p53-mediated transcription activation of p21/CDKN1A and Gadd45a, and subsequently delays G2-cell cycle arrest
malfunction
acetyl-CoA levels are elevated in NuA4 mutants
malfunction
deletion of Gcn5 or PCAF do not affect Treg development or suppressive function in vitro, but do affect inducible Treg (iTreg) development, and in vivo, abrogate Treg-dependent allograft survival. Deletion of either CBP or p300 results in only a modest decrease in Treg suppressive function. Activated CD4+T cell population in mesenteric lymph nodes of PCAF-/- mice, contribution of PCAF to iTreg development. PCAF deletion in Foxp3+ Treg cells causes lethal autoimmunity
malfunction
deletion of Gcn5 or PCAF do not affect Treg development or suppressive function in vitro, but do affect inducible Treg (iTreg) development, and in vivo, abrogate Treg-dependent allograft survival. Mice lacking GCN5 show prolonged allograft survival, suggesting this HAT might be a target for epigenetic therapy in allograft recipients. Dual deletion of GCN5 and PCAF leads to decreased Treg stability and numbers in peripheral lymphoid tissues, and mice succumbed to severe autoimmunity by 3-4 weeks of life. Conditional deletion of GCN5 in the Tregs of GCN5flfFoxp3YFP-cre mice have no significant effect on T-cell numbers or their baseline level of immune activation. GCN5 deletion also decreases Teff cell functions in vivo. GCN5 deletion in Foxp3+ Treg cells causes lethal autoimmunity
malfunction
enzyme deficiency is associated with congenital malformations and embryolethality. Enzyme inhibition induces oxidative stress
malfunction
enzyme inhibition induces cellular senescence
malfunction
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GCN5 deletion differently affects the growth of two strains, i.e. W303-1A and D273-10B/A1. The defective mitochondrial phenotype is related to a marked decrease in mtDNA content, which also involves the deletion of specific regions of the molecule. W303-1A cells deleted of the GCN5 gene show a thermosensitive phenotype. The ratio of mtDNA to nuclear DNA is strongly decreased (50 times) in the W303-1A mutant cells compared to wild-type cells. This defect is not observed in the D273-10B/1A cells. The different level of mtDNA in the two gcn5DELTA strains is consistent with their different phenotypes and with the higher respiratory competence of W303-1A compared to D273-10B/A1 cells. Deletion of GCN5 differently affects fermentative and respirative growth. The dynamics of mtDNA depletion during cell duplication indicates the loss of specific regions
malfunction
GCN5 loss leads to a modest impairment in T cell development. The generation of iNKT cells, identified by TCRbeta antibody and NK1.1 or CD1d-alphaGalCer tetramer, is largely diminished in the thymus of GCN5 KO mice. This block cannot be compensated in the periphery, as indicated by a profound decrease in iNKT cell frequencies and numbers in the spleen and liver of GCN5 KO mice. Impaired iNKT cell development is unlikely due to elevated cell death, as annexin V-positive populations of iNKT cells in the thymus, spleen, and liver are indistinguishable between wild-type and GCN5 KO mice. Dramatic accumulation of iNKT cells at the stage 0 in thymus of Gcn5 knockout mice. Phenotype, overview. GCN5 knockdown inhibits EGR2 acetylation
malfunction
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 HBO1 misregulation is linked to uncontrolled proliferation
malfunction
homozygous enzyme loss leads to lethal hematopoietic failure in mice at an early postnatal stage. Enzyme loss in adult mice results in dramatic hematopoietic failure
malfunction
inhibition of hARD1/NAA10 autoacetylation by K136R mutation induces the drop of KAT activity, but not NAT activity. Heat-induced disruption of hARD1/NAA10 structure also diminishes its lysine acetylation activity
malfunction
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knockdown of the enzyme inhibits differentiation of mesenchymal stem cells into osteoblast cells. The impaired osteogenic differentiation by enzyme knockdown is blocked by inhibition of nuclear factor kappaB
malfunction
loss of GCN5 in vivo does not promote metabolic remodeling in mouse skeletal muscle. Skeletal muscle gene expression of metabolic, angiogenic, and mitochondrial genes is not affected by loss of GCN5. Loss of GCN5 does not affect myosin heavy chain (MHC) composition, and markers of skeletal muscle development are unaffected by loss of GCN5. Skeletal muscle maximal respiratory capacity and succinate dehydrogenase (SDH) enzyme activity are not affected by loss of GCN5. Loss of GCN5 does not affect mitochondrial content or adaptations to endurance exercise training
malfunction
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 Myst3 forms fusion proteins in acute myeloid leukemia
malfunction
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 Myst4 forms fusion proteins in acute myeloid leukemia
malfunction
NuA4 mutants induce the expression of the inositol-3-phosphate synthase gene, INO1, which leads to excessive accumulation of inositol, a key metabolite used for phospholipid biosynthesis, called an Opi- phenotype. High-throughput genomic screens have identified many other mutants that derepress INO1 transcription, besides Opil mutants, and cause excessive accumulation of inositol, including mutants of the NuA4 complex (EAF1, EAF3, EAF5, EAF7, YAF9, and ESA1). NuA4 mutants exacerbate the growth defects of sec14-1ts under inositol-depleted conditions. As NuA4 mutants exhibit a derepression of INO1 and excessive inositol production, or Opi- phenotype, NuA4 mutants suppress the growth defect in sec14-1ts under inositol-depleted conditions. Lipid droplet dynamics are impaired in eaf1DELTA cells. The eaf1DELTA mutant negative genetic interaction with sec14-1ts and the decreased lipid droplet staining in eaf1D originate from defects within the fatty acid biosynthesis pathway
malfunction
oligomerization results in the loss of KAT activity
malfunction
oocyte enzyme deletion results in female infertility, with follicle development failure in the secondary and preantral follicle stages. Enzyme deletion results in abnormal heterochromatin configurations in oocytes. Granulosa cell-specific deletion of the enzyme does not affect follicle development or female fertility
malfunction
profound survival defects are observed belonging to mutants lacking the rv0998 gene. The mt-pat deletion alters carbon metabolism and redox homeostasis in hypoxia. The DELTAmt-pat deletion mutant grows normally in aerobic conditions and reaches a similar cell density as wild-type Mycobacterium tuberculosis in hypoxic vials. Unlike wild-type cells or a complemented strain, the DELTAmt-pat mutant progressively loses viability once hypoxia is achieved, consistent with the phenotype predicted by TNseq. In contrast to wild-type Mycobacterium tuberculosis, the DELTAmt-pat mutant continues to incorporate 2-[13C]-glucose into the oxidative branch of TCA under hypoxic conditions. Impaired survival of the DELTAmt-pat mutant in hypoxia indicates that preferential utilization of reductive TCA reactions is important for maintaining viability
malfunction
the AuA acetylation level decreases dramatically when ARD1 is mutated at R82 and Y122. The phosphorylation level of AuA is decreased in cells overexpressing K75R/K125R mutant
malfunction
the compaction phenotype of the yfmK deletions is partially bypassed by the hbsK41Q allele. This partial bypass may be explained by the action of more than one acetyltransferase at K41 or that YfmK acts at multiple sites. YfmK also acts at K3, K18, and K80, while YdgE may also act at K86
malfunction
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 the dysregulation of the enzyme activity is implicated in many human pathologies such as cancer, neurological and inflammatory disorders
malfunction
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 the dysregulation of the enzyme activity is implicated in many human pathologies such as cancer, neurological and inflammatory disorders. An aberrant activity of Gcn5 can lead to uncontrolled cell cycle progression
malfunction
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 the dysregulation of the enzyme activity is implicated in many human pathologies such as cancer, neurological and inflammatory disorders. PCAF knockdown blocks the growth of urothelial cancer cells and reduces their invasive ability
malfunction
-
cells lacking RTT109 have a high level of CAG/CTG repeat contractions and a twofold increase in breakage at CAG/CTG repeats
-
malfunction
-
the compaction phenotype of the yfmK deletions is partially bypassed by the hbsK41Q allele. This partial bypass may be explained by the action of more than one acetyltransferase at K41 or that YfmK acts at multiple sites. YfmK also acts at K3, K18, and K80, while YdgE may also act at K86
-
malfunction
-
NuA4 mutants induce the expression of the inositol-3-phosphate synthase gene, INO1, which leads to excessive accumulation of inositol, a key metabolite used for phospholipid biosynthesis, called an Opi- phenotype. High-throughput genomic screens have identified many other mutants that derepress INO1 transcription, besides Opil mutants, and cause excessive accumulation of inositol, including mutants of the NuA4 complex (EAF1, EAF3, EAF5, EAF7, YAF9, and ESA1). NuA4 mutants exacerbate the growth defects of sec14-1ts under inositol-depleted conditions. As NuA4 mutants exhibit a derepression of INO1 and excessive inositol production, or Opi- phenotype, NuA4 mutants suppress the growth defect in sec14-1ts under inositol-depleted conditions. Lipid droplet dynamics are impaired in eaf1DELTA cells. The eaf1DELTA mutant negative genetic interaction with sec14-1ts and the decreased lipid droplet staining in eaf1D originate from defects within the fatty acid biosynthesis pathway
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malfunction
-
acetyl-CoA levels are elevated in NuA4 mutants
-
malfunction
-
GCN5 deletion differently affects the growth of two strains, i.e. W303-1A and D273-10B/A1. The defective mitochondrial phenotype is related to a marked decrease in mtDNA content, which also involves the deletion of specific regions of the molecule. W303-1A cells deleted of the GCN5 gene show a thermosensitive phenotype. The ratio of mtDNA to nuclear DNA is strongly decreased (50 times) in the W303-1A mutant cells compared to wild-type cells. This defect is not observed in the D273-10B/1A cells. The different level of mtDNA in the two gcn5DELTA strains is consistent with their different phenotypes and with the higher respiratory competence of W303-1A compared to D273-10B/A1 cells. Deletion of GCN5 differently affects fermentative and respirative growth. The dynamics of mtDNA depletion during cell duplication indicates the loss of specific regions
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malfunction
-
knockdown of GCN5 inhibits the osteogenic differentiation of and mineralization in mesenchymal stem cells. Impaired osteogenic differentiation by GCN5 knockdown is blocked by inhibition of NF-kappaB
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malfunction
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GCN5 loss leads to a modest impairment in T cell development. The generation of iNKT cells, identified by TCRbeta antibody and NK1.1 or CD1d-alphaGalCer tetramer, is largely diminished in the thymus of GCN5 KO mice. This block cannot be compensated in the periphery, as indicated by a profound decrease in iNKT cell frequencies and numbers in the spleen and liver of GCN5 KO mice. Impaired iNKT cell development is unlikely due to elevated cell death, as annexin V-positive populations of iNKT cells in the thymus, spleen, and liver are indistinguishable between wild-type and GCN5 KO mice. Dramatic accumulation of iNKT cells at the stage 0 in thymus of Gcn5 knockout mice. Phenotype, overview. GCN5 knockdown inhibits EGR2 acetylation
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malfunction
-
profound survival defects are observed belonging to mutants lacking the rv0998 gene. The mt-pat deletion alters carbon metabolism and redox homeostasis in hypoxia. The DELTAmt-pat deletion mutant grows normally in aerobic conditions and reaches a similar cell density as wild-type Mycobacterium tuberculosis in hypoxic vials. Unlike wild-type cells or a complemented strain, the DELTAmt-pat mutant progressively loses viability once hypoxia is achieved, consistent with the phenotype predicted by TNseq. In contrast to wild-type Mycobacterium tuberculosis, the DELTAmt-pat mutant continues to incorporate 2-[13C]-glucose into the oxidative branch of TCA under hypoxic conditions. Impaired survival of the DELTAmt-pat mutant in hypoxia indicates that preferential utilization of reductive TCA reactions is important for maintaining viability
-
malfunction
-
profound survival defects are observed belonging to mutants lacking the rv0998 gene. The mt-pat deletion alters carbon metabolism and redox homeostasis in hypoxia. The DELTAmt-pat deletion mutant grows normally in aerobic conditions and reaches a similar cell density as wild-type Mycobacterium tuberculosis in hypoxic vials. Unlike wild-type cells or a complemented strain, the DELTAmt-pat mutant progressively loses viability once hypoxia is achieved, consistent with the phenotype predicted by TNseq. In contrast to wild-type Mycobacterium tuberculosis, the DELTAmt-pat mutant continues to incorporate 2-[13C]-glucose into the oxidative branch of TCA under hypoxic conditions. Impaired survival of the DELTAmt-pat mutant in hypoxia indicates that preferential utilization of reductive TCA reactions is important for maintaining viability
-
malfunction
-
the dysregulated gene expression induced by garcinol inhibition of the enzyme significantly inhibits Toxoplasma tachyzoite replication without being toxic to the human host cell. Garcinol inhibits TgGCN5b KAT activity and reduces global lysine acetylation in vivo in treated parasites, including its preferred substrate, histone H3
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malfunction
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GCN5 deletion differently affects the growth of two strains, i.e. W303-1A and D273-10B/A1. The defective mitochondrial phenotype is related to a marked decrease in mtDNA content, which also involves the deletion of specific regions of the molecule. W303-1A cells deleted of the GCN5 gene show a thermosensitive phenotype. The ratio of mtDNA to nuclear DNA is strongly decreased (50 times) in the W303-1A mutant cells compared to wild-type cells. This defect is not observed in the D273-10B/1A cells. The different level of mtDNA in the two gcn5DELTA strains is consistent with their different phenotypes and with the higher respiratory competence of W303-1A compared to D273-10B/A1 cells. Deletion of GCN5 differently affects fermentative and respirative growth. The dynamics of mtDNA depletion during cell duplication indicates the loss of specific regions
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metabolism
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beta-site amyloid precursor protein-cleaving enzyme 1 (BACE1) is acetylated in seven lysine residues that face the lumen of the ER and ER Golgi intermediate compartment (ERGIC)
metabolism
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histone and non-histone protein acetylation is involved, directly and indirectly, in controlling the duration, strength and specificity of the NF-kappaB-activating signaling pathway at multiple levels. Overview of the NF-kB-signaling pathway. Different signaling pathways can interfere with one another by modulating the availability of HATs or HDACs for a particular transcription complex
metabolism
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high mobility group domain-containing protein And-1 overexpression stabilizes Gcn5 through protein-protein interactions in vivo
metabolism
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the ablation of Cullin4-RING E3 ubiquitin ligase CRL4 leads to the stabilization of isoform Gcn5 in cells with depleted And-1, and Cdc10-dependent transcript 2, i.e. Cdt2, serves as a substrate receptor protein of CRL4. Overexpression of Cdt2 reduces the isoform Gcn5 protein levels, and CRLCdt2 is sufficient to ubiquitinate Gcn5 both in vivo and in vitro. And-1 stabilizes Gcn5 by impairing the interaction between Gcn5 and CRLCdt2 and thereby preventing Gcn5 ubiquitination and degradation. The degradation of Gcn5 is not dependent on proliferating cell nuclear antigen
metabolism
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acetylation, which targets a broad range of histone and non-histone proteins, is a reversible mechanism and plays a critical role in eukaryotic genes activation/deactivation
metabolism
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acetylation, which targets a broad range of histone and non-histone proteins, is a reversible mechanism and plays a critical role in eukaryotic genes activation/deactivation
metabolism
alteration in the specific histone post-translational modification during autophagy affects the transcriptional regulation of autophagy-related genes and initiates a regulatory feedback loop,which serves as a key determinant of survival versus death responses upon autophagy induction
metabolism
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enzyme PCAF is involved in transactivation of Bcl-6 and Pax5 genes, resulting in down-regulation of Blimp-1 gene expression, and plays a key role in epigenetic regulation of B cell development
metabolism
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megakaryoblastic leukemia 1 (MKL1, also named MRTF-A), a myocardin-related transcription factor, and histone acetyltransferase p300 can synergistically augment the expression of atechol-O-methyltransferase COMT gene, increase the metabolic rate of estrogen, and thus reduce the proliferation of MCF-7 breast cancer cells stimulated by estrogen. Transactivation of COMT induced by MKL1 and p300 is mediated via MKL1-SRF-CArG-box signal transduction
metabolism
analysis of connections between NuA4, inositol, and Sec14, which is a phosphatidylinositol/phosphatidylcholine transfer protein. Overview of phospholipid metabolism. Sec14 (UniProt ID P24280) is an essential phospholipid-binding protein that coordinates the metabolism of phosphatidylinositol-4-phosphate with phosphatidylcholine (PC) at the Golgi to create a lipid environment necessary for trafficking events
metabolism
aurora kinase A colocalalizes with ARD1 during cell division and cell migration
metabolism
exogenous acetate and reduced expression of ACC1 decreases glucose-deprived stress granule formation
metabolism
exogenous acetate and reduced expression of ACC1 decreases glucose-deprived stress granule formation
metabolism
four KATs (CBP, PCAF, GCN5L2, HAT1) perform acetylation of histone H3 lysine 9 (H3K9ac) in multiple tissues across the torpor-arousal cycle, determination of protein levels
metabolism
HBO1 can be either ubiquitinated or act as an ubiquitin ligase. HBO1 acetyltransferase complexes and activity regulation, overview. The tumor suppressor p53, adipogenesis regulator FAD24 (factor for adipocyte differentiation 24, also called NOC3L) and cell cycle kinases CDK1, CDK2, CDK11 and PLK1 are linked to HBO1. Moreover, cell growth inhibitor Niam and homeobox protein SIX1 that potentiates the Warburg effect by interaction with HBO1 are also presented. HBO1 complexes mainly consist of accessory proteins MEAF6, ING4 or ING5, and two types of cofactors for chromatin binding: Jade-1/2/3 and BRPF1/2/3. HBO1 is associated with the key events of the cell cycle, especially in mitosis through physical interaction with PLK1 and CDK1. Acetylation and autoacetylation regulates HBO1 activity
metabolism
HBO1 can be either ubiquitinated or act as an ubiquitin ligase. HBO1 acetyltransferase complexes and activity regulation, overview. The tumor suppressor p53, adipogenesis regulator FAD24 (factor for adipocyte differentiation 24, also called NOC3L) and cell cycle kinases CDK1, CDK2, CDK11 and PLK1 are linked to HBO1. Moreover, cell growth inhibitor Niam and homeobox protein SIX1 that potentiates the Warburg effect by interaction with HBO1 are also presented. HBO1 complexes mainly consist of accessory proteins MEAF6, ING4 or ING5, and two types of cofactors for chromatin binding: Jade-1/2/3 and BRPF1/2/3. HBO1 is associated with the key events of the cell cycle, especially in mitosis through physical interaction with PLK1 and CDK1. Acetylation and autoacetylation regulates HBO1 activity
metabolism
in HeLa cells, ectopically overexpressed recombinant MYC-LC3 associates with endogenous KAT2A, but overexpressed Flag-KAT2A does not associate with SQSTM1. Gene silencing of SQSTM1 does not disrupt the association between KAT2A and LC3 in HeLa cells, suggesting that KAT2A physically interacts with LC3, and SQSTM1 is not involved in the interaction between KAT2A and LC3
metabolism
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 PCAF and Gcn5-mediated acetylation can be implicated in type 2 diabetes
metabolism
stress granule formation is a conserved cellular stress response. Elevated acetyl-CoA levels suppress the formation of glucose-deprived stress granules, decreased acetyl-CoA levels enhance stress granule formation upon glucose deprivation. NuA4 mutant cells exhibit reduced Pab1-GFP cytoplasmic foci upon glucose deprivation. Suppression of glucose-deprived stress granule formation by eaf7DELTA mutants is mediated by increased acetyl-CoA. Acc1 activity is reduced in eaf1DELTA cells
metabolism
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the enzyme regulates osteogenic differentiation of mesenchymal stem cells by inhibiting nuclear factor kappaB. The enzyme represses nuclear factor kappa B-dependent transcription and inhibits the nuclear factor kappaB signaling pathway
metabolism
two prototypical GNAT family members, GCN5 (general control nonrepressed-protein 5, lysine acetyltransferase (KAT)2a) and p300/CBP-associated factor (p300/CBP-associated factor (PCAF), Kat2b) contribute to Treg functions through partially distinct and partially overlapping mechanisms
metabolism
two prototypical GNAT family members, GCN5 (general control nonrepressed-protein 5, lysine acetyltransferase (KAT)2a) and p300/CBP-associated factor (p300/CBP-associated factor (PCAF), Kat2b) contribute to Treg functions through partially distinct and partially overlapping mechanisms. Transplants in mice lacking PCAF undergo acute allograft rejection. PCAF deletion also enhances anti-tumor immunity in immunocompetent mice. Dual deletion of GCN5 and PCAF leads to decreased Treg stability and numbers in peripheral lymphoid tissues, and mice succumbed to severe autoimmunity by 3-4 weeks of life
metabolism
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analysis of connections between NuA4, inositol, and Sec14, which is a phosphatidylinositol/phosphatidylcholine transfer protein. Overview of phospholipid metabolism. Sec14 (UniProt ID P24280) is an essential phospholipid-binding protein that coordinates the metabolism of phosphatidylinositol-4-phosphate with phosphatidylcholine (PC) at the Golgi to create a lipid environment necessary for trafficking events
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metabolism
-
exogenous acetate and reduced expression of ACC1 decreases glucose-deprived stress granule formation
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metabolism
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stress granule formation is a conserved cellular stress response. Elevated acetyl-CoA levels suppress the formation of glucose-deprived stress granules, decreased acetyl-CoA levels enhance stress granule formation upon glucose deprivation. NuA4 mutant cells exhibit reduced Pab1-GFP cytoplasmic foci upon glucose deprivation. Suppression of glucose-deprived stress granule formation by eaf7DELTA mutants is mediated by increased acetyl-CoA. Acc1 activity is reduced in eaf1DELTA cells
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physiological function
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ATAC2 not only carries out an enzymatic function but also plays an architectural role in the stability of mammalian ATAC
physiological function
ATAC2 not only carries out an enzymatic function but also plays an architectural role in the stability of mammalian ATAC
physiological function
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CBP regulates neurobehavioural development, the enzyme activity and histone acetylation is required for control of neural cortical precursor competency to differentiate, regulation via environmental factors
physiological function
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Esa1 catalytic HAT activity is essential in yeast binding acetyl-CoA or lysine substrates and positively regulating the activities of NuA4 and Piccolo NuA4, Esa1 is involved in DNA damage repair
physiological function
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Esa1 mediates increased H4 acetylation and enhanced chromatin remodeling complex RSC occupancy and histone eviction in coding sequences and stimulates the rate of transcription elongation by polymerase II
physiological function
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GCN5 has a general repressive effect on microRNAs, miRNAs, that guide sequence-specific posttranscriptional gene silencing, but is required for expression of a subset of MIRNA genes, overview
physiological function
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genome-wide increase in histone acetylation stimulates replication independently of transcription in follicle cells. Enok is essential for mushroom body development, the mushroom bodies are the sites of olfactory learning and memory and in this function equivalent to the mammalian brain. Mof is required for sex chromosome dosage compensation acting in the MSL complex
physiological function
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HBO1 histone acetylase is important for DNA replication licensing in a Cdt1-dependent manner, overview. HBO1 plays a direct role at replication origins as a coactivator of the Cdt1 licensing factor. As HBO1 is also a transcriptional coactivator, it has the potential to integrate internal and external stimuli to coordinate transcriptional responses with initiation of DNA replication. HBO1 is not required for Cdt1 association with replication origins
physiological function
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Hbo1 plays a role as chromatin factor serving as a positive regulator of DNA replication , chromatin structure plays an important role in DNA replication initiation
physiological function
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histone acetylation by the enzyme plays an integral role in the epigenetic regulation of gene expression
physiological function
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histone acetylation is one of the major epigenetic mechanisms to regulate gene expression. MOZ is essential for the generation and maintenance of hematopoietic stem cells and for the appropriate development of myeloid, erythroid and B-lineage cell progenitors. MOZ is also required for self-renewal of hematopoietic stem cells
physiological function
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histone acetyltransferases and deacetylases play critical roles in the regulation of chromatin structure and gene expression
physiological function
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histone and non-histone protein acetylation is involved, directly and indirectly, in controlling the duration, strength and specificity of the NF-kappaB-activating signaling pathway at multiple levels. Overview of the NF-kB-signaling pathway, IkappaBalpha and some members of the IKK complex have a nuclear function involving HAT and HDAC recruitment
physiological function
intrinsic HAT activity of p300 plays an important role in the transcriptional coactivation of CREB, c-Jun, c-Fos, c-Myb, p53, Stats, nuclear receptors, RelA GATA, p73, and others. The enzyme is involved in post-translational modifications of chromatin that play a key role in the regulation of gene expression, cell growth, and differentiation
physiological function
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Mst1 is essentially required for damage response and chromosome segregation, it plays essential roles in maintenance of genome stability and recovery from DNA damage
physiological function
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MYST1 plays a role in tumor suppression mechanisms, functional composition and mechanisms of MYST1-containing complexes, overviewS
physiological function
MYST1 plays a role in tumor suppression mechanisms, functional composition and mechanisms of MYST1-containing complexes, overviewS
physiological function
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p300 plays a key role in NFkappaB subunit acetylation
physiological function
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Qkf/Morf requirement in neural stem cell/neural progenitor self-renewal with an additional role in some other cell types such as osteoblasts and germ cells. Qkf in adult neurogenesis in vivo, overview
physiological function
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role for Rtt109 and H3K56 acetylation in maintaining repetitive DNA sequences in Saccharomyces cerevisiae
physiological function
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Rtt109 is important for repairing replication-associated lesions and has functions in addition to maintaining genome stability
physiological function
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Rtt109 is important for yeast model organisms to survive DNA damage and maintain genome integrity, and Rtt109 is particularly important for fungal pathogenicity
physiological function
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Sas2 is required for subtelomeric reporter transgene silencing, but also for transcriptional activity of transgenes integrated into rDNA, for transcriptional activation of a mutated HMRE silent mating type locus and for protection of euchromatin from heterochromatin spreading
physiological function
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the enzyme activity of MOZ is critical for the proliferation of hematopoietic precursors, overview
physiological function
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the SAGA complex contains the histone ubiquitin protease Ubp8 and the histone acetyltransferase Gcn5 and is responsible for efficient transcription of SAGA regulated genes such as GAL1 and ADH2
physiological function
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Tip60 plays multiple roles in chromatin remodeling processes. Tip60 is a partner of the epigenetic integration platform interplayed by UHRF1, DNMT1 and HDAC1 involved in the epigenetic code replication
physiological function
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a histone modifying complex, composed of the Lsy-12 MYST-type histone acetyltransferase, the Ing-family plant homeodomain protein Lsy-13, and plant homeodomain/bromodomain protein Lin-49, is required to first initiate and then actively maintain lateralized gene expression in the gustatory system. A combination of transcription factors, which recognize DNA in a sequence-specific manner, and a histone modifying enzyme complex are responsible for inducing and maintaining neuronal laterality. In lsy-12 mutants the normally ASER-specific gcy-5 gene is expressed bilaterally from the onset of its expression in threefold embryos
physiological function
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co-expression of histone acetyltransferase E1A binding protein p300 dramatically enhances Pax5-mediated transcriptional activation. The p300-mediated enhancement is dependent on its intrinsic histone acetyltransferase activity. Moreover, p300 interacts with the C terminus of Pax5 and acetylates multiple lysine residues within the paired box DNA-binding domain of Pax5. Mutations of lysine residues 67 and 87/89 to alanine within Pax5 abolish p300-mediated enhancement of Pax5-induced Luc-CD19 reporter expression in HEK-293 cells
physiological function
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coexpressing isoform TIP60 decreases the transcriptional activation ability of c-Myb in functional reporter assays. TIP60 binds to the c-Myb target gene c-Myc promoter in a c-Myb-dependent manner. Knockdown of isoform Tip60 expression by siRNA increases endogenous c-Myc expression. c-Myb is associated with histone deacetylases HDAC1 and HDAC2, known to interact with TIP60 and repress transcription
physiological function
enzyme is essential for asexual intraerythrocytic growth. Overexpression of the long, active or a truncated, non-active version of the protein by stable integration of the expression cassette in the parasite genome results in changes of H4 acetylation and cell cycle progression. Overexpressing parasites shows changes in sensitivity to DNA-damaging agents
physiological function
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high mobility group domain-containing protein And-1 forms a complex with both histone H3 and isoform Gcn5. Downregulation of And-1 results in Gcn5 degradation, leading to the reduction of histone H3K9 and H3K56 acetylation. And-1 overexpression stabilizes Gcn5 through protein-protein interactions in vivo. And-1 expression is increased in cancer cells in a manner correlating with increase in Gcn5 and acetylation of H3K9 and H3K56
physiological function
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histone acetyltransferase CLOCK is a component of the transcriptional complex that includes transcriptional factor TFIID, and infected cell proteins ICP4, ICP27, and ICP22. CLOCK histone acetyltransferase is a component of the viral transcriptional machinery throughout the replicative cycle of the virus and ICP27 and ICP22 initiate their involvement in viral gene expression as components of viral transcriptome
physiological function
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histone acetyltransferase Mof plays an essential role in the maintenance of embryonic stem cell self-renewal and pluripotency. Embryonic stem cells with Mof deletion lose characteristic morphology, alkaline phosphatase staining, and differentiation potential. They also have aberrant expression of the core transcription factors Nanog, Oct4, and Sox2. The phenotypes of Mof null embryonic stem cells can be partially suppressed by Nanog overexpression, supporting the idea that Mof functions as an upstream regulator of Nanog in embryonic stem cells. Mof is an integral component of the embryonic stem cell core transcriptional network and Mof primes genes for diverse developmental programs. Mof is also required for Wdr5 recruitment and histone H3K4 methylation at key regulatory loci
physiological function
isoform IDM1is a regulator of DNA demethylation. IDM1 is required for preventing DNA hypermethylation of highly homologous multicopy genes and other repetitive sequences that are normally targeted for active DNA demethylation by Repressor of Silencing 1 and related 5-methylcytosine DNA glycosylases. IDM1 binds methylated DNA at chromatin sites lacking histone H3K4 di- or trimethylation and acetylates H3 to create a chromatin environment permissible for 5-methylcytosine DNA glycosylases to function
physiological function
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MYST protein acetyltransferase activity requires active site lysine autoacetylation
physiological function
MYST protein acetyltransferase activity requires active site lysine autoacetylation
physiological function
plants homozygous for T-DNA disruption alleles of GCN5 encoding a histone acetyltransferase show diminished expression of cold-regulated genes COR during cold acclimation. H3 acetylation at COR gene promoters is stimulated upon cold acclimation in gcn5 plants as in wild type plants, but the decrease in nucleosome occupancy is diminished. Thus, GCN5 is not the enzyme responsible for histone acetylation at COR gene promoters during cold acclimation
physiological function
protein mediates establishment of leaf polarity independently of ASYMMETRIC LEAVES2 and the trans-acting small interfering RNA-related pathway. Treatment with an inhibitor of histone deacetylases causes additive polarity defects in as2-1 east1-1 mutant plants. Isoform ELO3 may be involved, independent of the HDAC pathway, in the determination of polarity
physiological function
targeted reduction of ELP3 specifically in the developing Drosophila nervous system leads to a hyperactive phenotype with increase in climbing and locomotor activities and sleep loss in the adult flies, a significant expansion in synaptic bouton number and axonal length and branching in the larval neuromuscular junction as well as the misregulation of genes involved in sleep, vesicle transport and fusion, and protein chaperone activity. Ubiquitous reduction of ELP3 results in lethality
physiological function
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transcriptional coactivator gcn5 gene replacement mutants show a mild growth deficiency. Gcn5 is required for adaptation to stresses mediated by KCl and CaCl2, calcoflour white, MnCl2 and caffeine. The histone acetyltransferase activity of Gcn5 is required for its role in stress response
physiological function
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transcriptional coactivytor gcn5 gene replacement mutants show a mild growth deficiency. Gcn5 is required for adaptation to stresses mediated by KCl and CaCl2, calcoflour white, MnCl2 and caffeine. The histone acetyltransferase activity of Gcn5 is required for its role in stress response. Gcn5-dependent KCl response genes include membrane transporter VMR1 and heat-shock-response gene SSA4. The FLO8 gene, which encodes a transcriptional regulator, is up-regulated in the mutant. During KCl stress adaptation, Gcn5 shows a tendency for redistribution from short genes to the transcribed regions of long genes
physiological function
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acetylation of histones in the promoter region is a key step in transcription initiation. histone acetyltransferase p300 promotes MKL1-mediated transactivation of catechol-O-methyltransferase gene. Histone acetyltransferase p300 is recruited to the promoters of certain cardiac and smooth muscle specific genes to enhance the transactivation activity of myocardin, which is a master regulator in cardiovascular differentiation and development
physiological function
an important role for PCAF in arteriogenesis. Enzyme PCAF modulates post-ischemic gene regulation
physiological function
autophagy is an evolutionarily conserved catabolic process involved in several physiological and pathological processes. Although primarily cytoprotective, autophagy can also contribute to cell death. The histone H4 lysine 16 acetyltransferase hMOF regulates the outcome of autophagy. Induction of autophagy by rapamycin is coupled to reduction of histone H4 lysine 16 acetylation through downregulation of the histone acetyltransferase hMOF
physiological function
Elp3 is the catalytic subunit of the well-conserved transcription elongator complex. Apicomplexa lack all other elongator subunits, suggesting that the Elp3 in these organisms plays a role independent of transcription. Enzyme TgElp3 is essential in Toxoplasma and must be positioned at the mitochondrial surface for parasite viability
physiological function
enzyme GCN5 is a lysine acetyltransferase that generally regulates gene expression, expression of GCN5 promotes cell growth and the G1/S phase transition in multiple lung cancer cell lines. The enzyme potentiates the growth of non-small cell lung cancer via promotion of E2F1, cyclin D1, and cyclin E1 expression. E2F1 associates with and recruits GCN5 to sites of DNA damage. E2F1 is required for the GCN5-mediated regulation of lung cancer cell growth and for theG1/S transition. Cyclin D1 and cyclin E1 are downstream targets of E2F1. GCN5 is enriched at the E2F1-binding site of the cyclin D1, cyclin E1, or E2F1 promoters
physiological function
enzyme GCN5b seems to be essential for Toxoplasma viability. GCN5b plays a central role in transcriptional and chromatin remodeling complexes. GCN5b has a non-redundant and indispensable role in regulating gene expression required during the Toxoplasma lytic cycle GCN5b is an essential driver of tachyzoite proliferation
physiological function
enzyme KAT6B has tumor suppressorlike properties in cancer cells and exerts its tumor-inhibitory role through a defined type of histone H3 Lys23 acetyltransferase activity
physiological function
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enzyme PCAF promotes cell apoptosis and functions as a hepatocellular carcinoma repressor through acetylation of histone H4 and inactivation of AKT signaling. Enzyme PCAF regulates acetylation of histone H4 and phosphorylation of AKT in HCC
physiological function
expression of p300, but not of CBP, is strongly correlated with the malignant character of hepatocellular carcinoma. CBP/p300 HAT activity has an important role in malignant transformation, proliferation, apoptotic sensitivity and invasion in hepatocellular carcinoma
physiological function
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GCN5 is an important histone acetyltransferase that is required for gene expression changes involved in numerous plant development pathways and responses to environmental conditions in Arabidopsis. Histone acetyltransferase GCN5 is essential for heat stress-responsive gene activation and thermotolerance in Arabidopsis thaliana
physiological function
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histone acetyltransferase PCAF is involved in transactivation of Bcl-6 and Pax5 genes in immature B cells. PCAF takes part in transcriptional activation of B cell lymphoma-6 (Bcl-6) and paired box gene 5 (Pax5), which are essential transcription factors for normal development of B cells. The enzyme regulates various epigenetic events for transcriptional regulation through alterations in the chromatin structure
physiological function
lysine acetylation is a critical post-translational modification that influences protein activity, stability, and binding properties. The acetylation of histone proteins in particular is a feature of gene expression regulation. TgGCN5b is the only nuclear GCN5-family KAT known to be required for Toxoplasma tachyzoite replication
physiological function
lysine acetyltransferase 8 is a histone acetyltransferase responsible for acetylating lysine 16 on histone H4 and plays a role in cell cycle progression as well as acetylation of the tumor suppressor protein p53
physiological function
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regulation of histone acetylation is fundamental to the utilization of eukaryotic genomes in chromatin. H4K16 acetylation is thought to affect the basic properties of the chromatin fiber. Male cells display twice the amount of H4K16 acetylation but reduced levels of several other acetylation motifs including H4K5, H4K12, and H3K14 acetylation as compared to female cells due to acetyltransferase MOF. Drosophila's histone acetylation system includes (1) the extensively studied model KATs (GCN5/PCAF, CBP/P300, MOF, HAT1, and TIP60), (2) less well characterized KATs (KAT6 [MOZ/MORF], HBO1, ELP3, TAF1, and ATAC2), (3) a mostly uncharacterized class of GCN5-related KATs (NAT6, NAT9, and NAT10), (4) N-terminal acetyltransferases suggested to also acetylate internal lysines (NAA10, NAA20, NAA30, NAA40, NAA50, and NAA60), (5) putative acetyltransferases with no recognizable direct homologue in non-Drosophilid species (CG5783 and CG12560), (6) the acetyltransferase ECO, and (7) a bifunctional enzyme containing a O-GlcNAcase activity and potentially a KAT activity (MGEA5, also known as NCOAT or OGA)
physiological function
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the enzyme GCN5 plays essential roles in various developmental processes, it has a critical function in osteogenic commitment of mesenchymal stem cells. In this role, the histone acetyltransferase activity of GCN5 is not required. Enzyme GCN5 represses nuclear factor kappa B-dependent transcription and inhibits the NF-kappaB signaling pathway. GCN5 is responsible for degradation of RelA. Acetylase activity of GCN5 is dispensable for the regulation of osteogenic differentiation of mesenchymal stem cells
physiological function
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the enzyme plays critical roles in apoptosis and DNA repair
physiological function
ARD1-mediated aurora kinase A (AuA) acetylation promotes cell proliferation and migration. ARD1-mediated AuA acetylation at K75/K125 enhances AuA kinase activity. Cells overexpressing AuA double mutant K75R/K125R display a dramatically decreased level of acetylated AuA, suggesting that these sites are critical for the acetylation of AuA by ARD1. AuA interacts with ARD1, and AuA acetylation is regulated by functional ARD1
physiological function
arrest defective 1 (ARD1), also known as N(alpha)-acetyltransferase 10 (NAA10) is originally identified as an N-terminal acetyltransferase (NAT) that catalyzes the acetylation of N-termini of newly synthesized peptides. Mammalian ARD1/NAA10 also plays a roleas lysine acetyltransferase (KAT) that posttranslationally acetylates internal lysine residues of proteins. ARD1/NAA10 is the only enzyme with both NAT (EC 2.3.1.255) and KAT (EC 2.3.1.48) activities. NATs acetylate N-terminal residues of newly synthesized proteins from ribosomes in an irreversible manner. N-terminal acetylation is known to be closely related to protein stability, interaction, and localization. lysine acetylation catalyzed by KATs is reversibly regulated by lysine deacetyltransferases (KDACs) that remove acetyl groups from lysine residues in proteins. While acetylation neutralizes the positive charge on lysine residues, deacetylation recovers it, thereby causing a change in electronic and conformational properties of proteins. Acetylation and deacetylation of lysine residues serve as the switches that turn-on and turn-off the cellular signal pathways and regulate diverse biological events. Any unbalance between lysine acetylation and deacetylation results in the improper regulation of biological processes and may cause various types of human diseases such as cancer and neurodegeneration
physiological function
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Asn is needed to regulate allosterically activity of SvePatA. Asp16 and Ser17 at the interface between beta1 and alpha1 may somehow affect the Cys binding of AmiPatA. Lys112 and Pro113 are not involved in the Asn binding of SvePatA. It is likely that the Pat enzymes are carefully regulated at the transcriptional and post-translational levels in response to changes of the intracellular signals that control the acetylation of specific proteins, which in turn mould the metabolic network. The relationship between the structure and function of SvePatA and AmiPatA showed that some amino acid residues at the interface between beta1-sheet and alpha1-helix may affect the ligand-binding activity. The archetypical acetyltransferases AAPatAs possessing GNAT and ACT domains show a novel signaling pathway for regulating the acetylation of cellular proteins. The acetylation level of proteins may be closely correlated with intracellular concentrations of Asn and Cys in Actinobacteria
physiological function
at least one physiological function of the acetylation of HBsu at key lysine residues by lysine acetyltransferase YfmK is to regulate nucleoid compaction, analogous to the role of histone acetylation in eukaryotes. Acetylation is a regulatory component of the function of HBsu in nucleoid compaction. HBsu belongs to the highly conserved HU family of nucleoid-associated proteins (NAPs) and is essential for viability in Bacillus subtilis. In bacteria, the NAPs are largely responsible for chromosome compaction
physiological function
conserved role for Tip60, the mammalian homologue of Saccharomyces cerevisiae Esa1, in the regulation of stress granules in human breast cancer cells. Stress granule formation is a conserved cellular stress response. Tip60 affects stress granule levels in mammalian cells
physiological function
enzyme HBO1 is responsible for the bulk acetylation of histone H4 and H3K14. HBO1 functions as the core catalytic subunit in multimeric complexes established by cofactors and accessory proteins. HBO1 affords multiple functions in various processes such as DNA replication, gene transcription, protein ubiquitination, immune regulation, stem cell pluripotent and self-renewal maintenance as well as embryonic development. HBO1 functions as the core catalytic subunit in multimeric complexes established by cofactors and accessory proteins. HBO1 is reported to participate in transcriptional regulation in alternative complexes such as HBO1-SIX1 and HBO1-Niam. HBO1 encourages tissue-specific gene expression, for it participates in intragenic histone acetylation and mediated Pol II binding in regulating the expression of endothelial VEGFR-2. HBO1-mediated histone acetylation enables the accession of transcriptional factors to the chromatin and regulates the initiation of transcription. Alternatively, HBO1 complexes occupies the coding region to afford a direct role in transcriptional elongation. HBO1 might acetylate the transcriptional factors and change their protein-protein interactions. HBO1 facilitates chromatin loading of minichromosome maintenance (MCM) complexes and promotes DNA replication licensing. Loading of MCM complexes to chromatin is the final step of the prereplicative complexes assembly. Indispensable roles of HBO1 in chromosome remodeling and DNA replication, the mechanism regarding how HBO1 facilitates MCM loading and the involved protein-protein interactions is analyzed. HBO1 is required for T cell development and immune regulation. HBO1 acetyltransferase complexes and activity regulation, overview. Multiple functions of HBO1 are realized by the formation of protein complexes with different cofactors or partner proteins. The components of HBO1 acetyltransferase complexes and related downstream pathways may also contribute to the activity of HBO1 in cell proliferation. For example, Jade-2-mediated HBO1 acetylation activity enhances the expression of mechano-transductor signaling factor YAP1 to modulate cell elasticity in ovarian cancer. Besides, mutations in ING4 or ING5 destabilize the protein and contribute to tumorigenesis. HBO1 is essential for global acetylation of histone H3K4 and H4, thus the acetylation activity of HBO1 may also induce the expression of anti-cancer genes such as Brahma. In acute myeloid leukemia, HBO1 expression is suppressed associated with the decease of global H4K5 acetylation. Interestingly, a fusion of nucleoporin-98 (NUP98)-HBO1 is identified in a patient with chronic myelomonocytic leukemia (CMML). NUP98-HBO1 is sufficient to generate CMML pathogenesis through aberrant histone acetylation on the promoter of oncogene such as HOXA9
physiological function
enzyme HBO1 is responsible for the bulk acetylation of histone H4 and H3K14. HBO1 functions as the core catalytic subunit in multimeric complexes established by cofactors and accessory proteins. HBO1 affords multiple functions in various processes such as DNA replication, gene transcription, protein ubiquitination, immune regulation, stem cell pluripotent and self-renewal maintenance as well as embryonic development. HBO1 functions as the core catalytic subunit in multimeric complexes established by cofactors and accessory proteins. HBO1 is reported to participate in transcriptional regulation in alternative complexes such as HBO1-SIX1 and HBO1-Niam. HBO1 encourages tissue-specific gene expression, for it participates in intragenic histone acetylation and mediated Pol II binding in regulating the expression of endothelial VEGFR-2. HBO1-mediated histone acetylation enables the accession of transcriptional factors to the chromatin and regulates the initiation of transcription. Alternatively, HBO1 complexes occupies the coding region to afford a direct role in transcriptional elongation. HBO1 might acetylate the transcriptional factors and change their protein-protein interactions. HBO1 facilitates chromatin loading of minichromosome maintenance (MCM) complexes and promotes DNA replication licensing. Loading of MCM complexes to chromatin is the final step of the prereplicative complexes assembly. Indispensable roles of HBO1 in chromosome remodeling and DNA replication, the mechanism regarding how HBO1 facilitates MCM loading and the involved protein-protein interactions is analyzed. HBO1 is required for T cell development and immune regulation. HBO1 acetyltransferase complexes and activity regulation, overview. Multiple functions of HBO1 are realized by the formation of protein complexes with different cofactors or partner proteins. HBO1 functions in spermatogenesis
physiological function
enzyme TgGCN5b is the only nuclear GCN5 family KAT known to be required for Toxoplasma tachyzoite replication
physiological function
GCN5-related N-acetyltransferases (GNATs) are a large and diverse group of enzymes which catalyze the transfer of an acetyl group from acetyl coenzyme A (Ac-CoA) to the amine group of a substrate. Substrates include protein N-terminus, lysine of histone tails, and other small molecules such as aminoglycoside, serotonin, and glucose-6-phosphate
physiological function
histone acetyltransferases (HATs) play critical roles in controlling T-regulation (Treg) development
physiological function
histone acetyltransferases (HATs) play critical roles in controlling T-regulation (Treg) development. PCAF helps protect Tregs from undergoing apoptosis upon TCR stimulation
physiological function
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in Saccharomyces cerevisiae the lysine-acetyltransferase Gcn5 (KAT2) is part of the SAGA complex and is responsible for histone acetylation widely or at specific lysines. In wild-type mitochondria the Gcn5 protein is present in the mitoplasts, suggesting a distinct mitochondrial function for Gcn5 independent from the SAGA complex and possibly another function for this protein connecting epigenetics and metabolism, role of Gcn5 as a factor involved in respiratory metabolism, overview
physiological function
KAT6A suppresses cellular senescence through the regulation of suppressors of the CDKN2A locus, a function that requires its KAT activity
physiological function
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts
physiological function
lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts
physiological function
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. Enzyme CBP is implicated in Rubinstein-Taybi syndrome and inflammation, and forms fusion proteins in acute myeloid leukemia
physiological function
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. Enzyme CLOCK is a regulator of circadian rhythm
physiological function
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. Enzyme p300 is implicated in inflammation, esophageal squamous cell and hepatocellular carcinoma, and it forms fusion proteins in acute myeloid leukemia. The acetylase activity regulated by autoacetylation
physiological function
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. Enzyme SCR1 is involved in steroid-related transcription through pre-initiation complex formation stabilization. SRC1 KAT activity is primarily specific for histones H3 and H4, and is a consequence of ligand binding to steroid receptors. This is thought to be a mechanism by which steroid receptors and their co-activators enhance formation of a stable pre-initiation complex, thereby increasing transcription of the target genes
physiological function
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. GCN5 is upregulated in non-small cell lung carcinoma, colon cancer, and glioma, and implicated in type 2 diabetes and AIDS. Gcn5 is essential in the activation and stabilization of the tumor suppressor p53. It acetylates peroxisome proliferator-activated receptor gamma co-activator 1alpha (PGC-1alpha), a co-activator which plays a central role in hepatic gluconeogenesis. PGC-1alpha acetylation triggers its degradation, leading to a decrease in blood and hepatic glucose output. In non-small-cell lung cancer (NSCLC), Gcn5 promotes cell proliferation by regulating the expression of cell cycle proteins cyclin D1, E1 and E2F1. In colon cancer tissues, Gcn5 overexpression is found to be dependent on both the cell cycle protein E2F1 and the oncogene c-myc
physiological function
lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. MYST enzymes have their acetylase activity regulated by autoacetylation. Tip60 activates the machinery for DNA repair
physiological function
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. MYST enzymes have their acetylase activity regulated by autoacetylation. Tip60 activates the machinery for DNA repair. It is involved in numerous activities such as transcription, DNA damage cellular response, apoptosis and it has been reported to regulate p53 through acetylation at Lys120
physiological function
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. PCAF acetylates the cyclin-dependent kinase inhibitor p27 leading to its degradation and facilitating cell cycle progression. PCAF is essential in the activation and stabilization of the tumor suppressor p53. It acetylates peroxisome proliferator-activated receptor gamma co-activator 1alpha (PGC-1alpha), a co-activator which plays a central role in hepatic gluconeogenesis. PGC-1alpha acetylation triggers its degradation, leading to a decrease in blood and hepatic glucose output. PCAF catalyzes the acetylation of the oncosuppressor protein PTEN on two lysine residues (Lys125 and Lys128), thereby promoting cell cycle blocking in the G1 phase after growth factor stimulation. A critical function of PCAF is the acetylation of connexin 43, which is linked to cardiac dystrophy. PCAF catalyzes the acetylation of the oncosuppressor protein PTEN on two lysine residues (Lys125 and Lys128), thereby promoting cell cycle blocking in the G1 phase after growth factor stimulation. PCAF is implicated in urothelial cancer, type 2 diabetes and cardiac dystrophy
physiological function
lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. Rtt109 has a low catalytic efficiency in isolation, but it is much more active when associated with the histone chaperones Asf1 and Vps75. The two chaperones also determine substrate specificity, with the preferred substrate being H3K56 when Rtt109 is associated with Asf1, whereas H3K9 and H3K23 are acetylated when in complex with Vps75
physiological function
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. TAF1 is a regulatory element in hormone-related transcriptional processes
physiological function
lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. TAF1 is a regulatory element in hormone-related transcriptional processes
physiological function
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. The enzyme is a regulatory element in hormone-related transcriptional processes. It is required for RNA polymerase III transcription
physiological function
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. The MYST protein HBO1/MYST2 preferentially catalyzes the acetylation of histone H4. MYST enzymes have their acetylase activity regulated by autoacetylation. Enzyme HBO1/MYST2 is involved in regulation of DNA replication, since it interacts with proteins of the origin of replication complex (ORC1). HBO1 is involved in DNA replication
physiological function
lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. The MYST protein MOF catalyzes the acetylation of p53 at lysine120, which helps to discriminate cell-cycle arrest and apoptotic functions. MYST enzymes have their acetylase activity regulated by autoacetylation
physiological function
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. The MYST protein MOF catalyzes the acetylation of p53 at lysine120, which helps to discriminate cell-cycle arrest and apoptotic functions. MYST enzymes have their acetylase activity regulated by autoacetylation. MYST1/MOF is associated with tumor growth of oral tongue squamous cell carcinoma
physiological function
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. The MYST protein MORF catalyzes the acetylation of histone H3 at Lys14. MYST enzymes have their acetylase activity regulated by autoacetylation
physiological function
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. The MYST protein MOZ catalyzes the acetylation of histone H3 at Lys14. MYST enzymes have their acetylase activity regulated by autoacetylation
physiological function
lysine acetyltransferase GCN5 is a regulator of mitochondrial biogenesis via its inhibitory action on peroxisome proliferator activated receptor-gamma coactivator-1alpha (PGC-1alpha). Specific contribution of GCN5 to skeletal muscle metabolism and mitochondrial adaptations to endurance exercise in vivo
physiological function
lysine acetyltransferases (KATs) play a crucial role in modulating the expression and activity of a wide-variety of cellular pathways and processes, and therefore, may play a role during hibernation when the cell is shifting to an energy conservative, cytoprotective state. Roles for lysine acetyltransferases during mammalian hibernation
physiological function
lysine acetyltransferases GCN5 is a transcription-related histone acetyltransferase. GCN5 is a specific lysine acetyltransferase of EGR2, a transcription factor required for CD1d-restricted invariant natural killer T (iNKT) cell development. The histone acetyltransferase GCN5 is essential for iNKT cell development during the maturation stage. GCN5-mediated acetylation positively regulated EGR2 transcriptional activity, and both genetic and pharmacological GCN5 suppression specifically inhibits the transcription of EGR2 target genes in iNKT cells, including Runx1, PLZF, IL-2Rb, and T-bet. Therefore, GCN5-mediated EGR2 acetylation is a molecular mechanism that regulates iNKT development. GCN5 has been shown to play critical roles in a variety of important biological functions including metabolic regulation, cell growth and survival, DNA damage repair, and embryonic development. Role of GCN5 in T cell immunity, overview. GCN5 is required for the development of iNKT cells in mice. GCN5 regulates the expression of genes driving iNKT development through EGR2
physiological function
N-terminal acetylation catalyzed by NATs is one of the most common protein modifications in eukaryotes, affecting about 80% human proteins. In general, NATs acetylate N-terminal residues of newly synthesized proteins from ribosomes in an irreversible manner. N-terminal acetylation is known to be closely related to protein stability, interaction, and localization. Human ARD1/NAA10 expanded its' role to lysine acetyltransferase (KAT) that post-translationally acetylates internal lysine residues of proteins. Size-exclusion analysis reveals that most recombinant hARD1/NAA10 forms oligomers. While oligomeric recombinant hARD1/NAA10 loses its ability for lysine acetylation, its monomeric form clearly exhibits lysine acetylation activity in vitro. In contrast to N-terminal acetylation, lysine acetylation catalyzed by KATs is reversibly regulated by lysine deacetyltransferases (KDACs) that remove acetyl groups from lysine residues in protein. hARD1 regulates a wide range of cellular functions, including cell cycle, apoptosis, migration, stress response, and differentiation. NAT and KAT activity might be independently regulated, relying on the interaction partners
physiological function
p300 and GCN5 are two representative lysine acetyltransferases (KATs) in mammalian cells. They possess multiple acyltransferase activities including acetylation, propionylation, and butyrylation of the epsilon-amino group of lysine residues of histones and non-histone protein substrates. The protein substrates are extensively involved in various biological events including gene expression, cell cycle, and cellular metabolism. Canonical KAT-related processes such as gene expression, DNA repair, cell cycle, and apoptosis involve both known and newly identified substrates of p300 and GCN5, overview
physiological function
protein acetyl-transferase MtPat promotes survival and alters the flux of carbon from oxidative to reductive TCA reactions. Essentiality of Mt-Pat in hypoxia, role for Mt-Pat orthologues in regulating acyl-CoA ligases. Mt-Pat orthologues function to regulate the formation of acetyl-CoA. The absence of this regulation in hypoxia results in continual flux of this metabolite into oxidative TCA reactions
physiological function
protein acetylation catalyzed by specific histone acetyltransferases (HATs) is an essential posttranslational modification (PTM) and involved in the regulation a broad spectrum of biological processes in eukaryotes
physiological function
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the activity of AmiPatA is regulated allosterically by Cys binding. It is likely that the Pat enzymes are carefully regulated at the transcriptional and post-translational levels in response to changes of the intracellular signals that control the acetylation of specific proteins, which in turn mould the metabolic network. The relationship between the structure and function of SvePatA and AmiPatA showed that some amino acid residues at the interface between beta1-sheet and alpha1-helix may affect the ligand-binding activity. The archetypical acetyltransferases AAPatAs possessing GNAT and ACT domains show a novel signaling pathway for regulating the acetylation of cellular proteins. The acetylation level of proteins may be closely correlated with intracellular concentrations of Asn and Cys in Actinobacteria
physiological function
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the enzyme downregulates biofilm formation in Acinetobacter baumannii via polyamine acetylation
physiological function
the enzyme has an essential function in oogenesis and is essential for female fertility by regulating antioxidant gene expression. The enzyme directly regulates antioxidant gene expression in oocytes
physiological function
the enzyme is a developmental-stage-specific chromatin regulator whose activity is essential for adult but not early and midgestational murine hematopoietic maintenance. Enzyme activity is required for adult hematopoietic cell survival
physiological function
the enzyme is required for embryonic development
physiological function
the histone acetyltransferase KAT2A/GCN5 (lysine acetyltransferase 2) acetylates TUBA in vascular smooth muscle cells leading to microtubule instability and promotion of VSMC migration. Deacetylation of TUBA and perturbation of microtubule stability via selective autophagic degradation of KAT2A are essential for autophagy-promoting VSMC migration
physiological function
the lysine acetyltransferase complex NuA4 plays a role in phospholipid homeostasis. One role for NuA4 is the regulation of chromatin remodeling and gene transcription through the acetylation of histones H4 andH2A-Z, and NuA4 also targets nonhistone proteins
physiological function
the Saccharomyces cerevisiae lysine acetyltransferase complex NuA4 is required for stress granule (SG) formation upon glucose deprivation but not heat stress. The impact of NuA4 on glucose-deprived stress granule formation is partially mediated through regulation of acetyl-CoA levels via the acetyl-CoA carboxylase Acc1. Both NuA4 and the metabolite acetyl-CoA are critical signaling pathways regulating the formation of glucose-deprived stress granules. Functionally redundant roles for Eaf7 and Gcn5 in SG formation upon glucose deprivation, overview. NuA4 is required for glucose deprivation stress granule formation but does not impact processing bodies. NuA4 does not regulate the formation of stress granules through the inhibition of translation initiation or the Snf1 pathway. Eaf1 and Eaf7 are not required for the inhibition of translation initiation upon 10 minutes glucose deprivation
physiological function
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GCN5-related N-acetyltransferases (GNATs) are a large and diverse group of enzymes which catalyze the transfer of an acetyl group from acetyl coenzyme A (Ac-CoA) to the amine group of a substrate. Substrates include protein N-terminus, lysine of histone tails, and other small molecules such as aminoglycoside, serotonin, and glucose-6-phosphate
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physiological function
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role for Rtt109 and H3K56 acetylation in maintaining repetitive DNA sequences in Saccharomyces cerevisiae
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physiological function
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Asn is needed to regulate allosterically activity of SvePatA. Asp16 and Ser17 at the interface between beta1 and alpha1 may somehow affect the Cys binding of AmiPatA. Lys112 and Pro113 are not involved in the Asn binding of SvePatA. It is likely that the Pat enzymes are carefully regulated at the transcriptional and post-translational levels in response to changes of the intracellular signals that control the acetylation of specific proteins, which in turn mould the metabolic network. The relationship between the structure and function of SvePatA and AmiPatA showed that some amino acid residues at the interface between beta1-sheet and alpha1-helix may affect the ligand-binding activity. The archetypical acetyltransferases AAPatAs possessing GNAT and ACT domains show a novel signaling pathway for regulating the acetylation of cellular proteins. The acetylation level of proteins may be closely correlated with intracellular concentrations of Asn and Cys in Actinobacteria
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physiological function
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at least one physiological function of the acetylation of HBsu at key lysine residues by lysine acetyltransferase YfmK is to regulate nucleoid compaction, analogous to the role of histone acetylation in eukaryotes. Acetylation is a regulatory component of the function of HBsu in nucleoid compaction. HBsu belongs to the highly conserved HU family of nucleoid-associated proteins (NAPs) and is essential for viability in Bacillus subtilis. In bacteria, the NAPs are largely responsible for chromosome compaction
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physiological function
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the lysine acetyltransferase complex NuA4 plays a role in phospholipid homeostasis. One role for NuA4 is the regulation of chromatin remodeling and gene transcription through the acetylation of histones H4 andH2A-Z, and NuA4 also targets nonhistone proteins
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physiological function
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the Saccharomyces cerevisiae lysine acetyltransferase complex NuA4 is required for stress granule (SG) formation upon glucose deprivation but not heat stress. The impact of NuA4 on glucose-deprived stress granule formation is partially mediated through regulation of acetyl-CoA levels via the acetyl-CoA carboxylase Acc1. Both NuA4 and the metabolite acetyl-CoA are critical signaling pathways regulating the formation of glucose-deprived stress granules. Functionally redundant roles for Eaf7 and Gcn5 in SG formation upon glucose deprivation, overview. NuA4 is required for glucose deprivation stress granule formation but does not impact processing bodies. NuA4 does not regulate the formation of stress granules through the inhibition of translation initiation or the Snf1 pathway. Eaf1 and Eaf7 are not required for the inhibition of translation initiation upon 10 minutes glucose deprivation
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physiological function
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Elp3 is the catalytic subunit of the well-conserved transcription elongator complex. Apicomplexa lack all other elongator subunits, suggesting that the Elp3 in these organisms plays a role independent of transcription. Enzyme TgElp3 is essential in Toxoplasma and must be positioned at the mitochondrial surface for parasite viability
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physiological function
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GCN5-related N-acetyltransferases (GNATs) are a large and diverse group of enzymes which catalyze the transfer of an acetyl group from acetyl coenzyme A (Ac-CoA) to the amine group of a substrate. Substrates include protein N-terminus, lysine of histone tails, and other small molecules such as aminoglycoside, serotonin, and glucose-6-phosphate
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physiological function
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GCN5-related N-acetyltransferases (GNATs) are a large and diverse group of enzymes which catalyze the transfer of an acetyl group from acetyl coenzyme A (Ac-CoA) to the amine group of a substrate. Substrates include protein N-terminus, lysine of histone tails, and other small molecules such as aminoglycoside, serotonin, and glucose-6-phosphate
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physiological function
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in Saccharomyces cerevisiae the lysine-acetyltransferase Gcn5 (KAT2) is part of the SAGA complex and is responsible for histone acetylation widely or at specific lysines. In wild-type mitochondria the Gcn5 protein is present in the mitoplasts, suggesting a distinct mitochondrial function for Gcn5 independent from the SAGA complex and possibly another function for this protein connecting epigenetics and metabolism, role of Gcn5 as a factor involved in respiratory metabolism, overview
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physiological function
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GCN5-related N-acetyltransferases (GNATs) are a large and diverse group of enzymes which catalyze the transfer of an acetyl group from acetyl coenzyme A (Ac-CoA) to the amine group of a substrate. Substrates include protein N-terminus, lysine of histone tails, and other small molecules such as aminoglycoside, serotonin, and glucose-6-phosphate
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physiological function
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GCN5-related N-acetyltransferases (GNATs) are a large and diverse group of enzymes which catalyze the transfer of an acetyl group from acetyl coenzyme A (Ac-CoA) to the amine group of a substrate. Substrates include protein N-terminus, lysine of histone tails, and other small molecules such as aminoglycoside, serotonin, and glucose-6-phosphate
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physiological function
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GCN5-related N-acetyltransferases (GNATs) are a large and diverse group of enzymes which catalyze the transfer of an acetyl group from acetyl coenzyme A (Ac-CoA) to the amine group of a substrate. Substrates include protein N-terminus, lysine of histone tails, and other small molecules such as aminoglycoside, serotonin, and glucose-6-phosphate
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physiological function
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the enzyme GCN5 plays essential roles in various developmental processes, it has a critical function in osteogenic commitment of mesenchymal stem cells. In this role, the histone acetyltransferase activity of GCN5 is not required. Enzyme GCN5 represses nuclear factor kappa B-dependent transcription and inhibits the NF-kappaB signaling pathway. GCN5 is responsible for degradation of RelA. Acetylase activity of GCN5 is dispensable for the regulation of osteogenic differentiation of mesenchymal stem cells
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physiological function
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the enzyme activity of MOZ is critical for the proliferation of hematopoietic precursors, overview
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physiological function
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lysine acetyltransferases GCN5 is a transcription-related histone acetyltransferase. GCN5 is a specific lysine acetyltransferase of EGR2, a transcription factor required for CD1d-restricted invariant natural killer T (iNKT) cell development. The histone acetyltransferase GCN5 is essential for iNKT cell development during the maturation stage. GCN5-mediated acetylation positively regulated EGR2 transcriptional activity, and both genetic and pharmacological GCN5 suppression specifically inhibits the transcription of EGR2 target genes in iNKT cells, including Runx1, PLZF, IL-2Rb, and T-bet. Therefore, GCN5-mediated EGR2 acetylation is a molecular mechanism that regulates iNKT development. GCN5 has been shown to play critical roles in a variety of important biological functions including metabolic regulation, cell growth and survival, DNA damage repair, and embryonic development. Role of GCN5 in T cell immunity, overview. GCN5 is required for the development of iNKT cells in mice. GCN5 regulates the expression of genes driving iNKT development through EGR2
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physiological function
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lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts
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physiological function
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lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. Rtt109 has a low catalytic efficiency in isolation, but it is much more active when associated with the histone chaperones Asf1 and Vps75. The two chaperones also determine substrate specificity, with the preferred substrate being H3K56 when Rtt109 is associated with Asf1, whereas H3K9 and H3K23 are acetylated when in complex with Vps75
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physiological function
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protein acetyl-transferase MtPat promotes survival and alters the flux of carbon from oxidative to reductive TCA reactions. Essentiality of Mt-Pat in hypoxia, role for Mt-Pat orthologues in regulating acyl-CoA ligases. Mt-Pat orthologues function to regulate the formation of acetyl-CoA. The absence of this regulation in hypoxia results in continual flux of this metabolite into oxidative TCA reactions
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physiological function
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protein acetyl-transferase MtPat promotes survival and alters the flux of carbon from oxidative to reductive TCA reactions. Essentiality of Mt-Pat in hypoxia, role for Mt-Pat orthologues in regulating acyl-CoA ligases. Mt-Pat orthologues function to regulate the formation of acetyl-CoA. The absence of this regulation in hypoxia results in continual flux of this metabolite into oxidative TCA reactions
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physiological function
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the activity of AmiPatA is regulated allosterically by Cys binding. It is likely that the Pat enzymes are carefully regulated at the transcriptional and post-translational levels in response to changes of the intracellular signals that control the acetylation of specific proteins, which in turn mould the metabolic network. The relationship between the structure and function of SvePatA and AmiPatA showed that some amino acid residues at the interface between beta1-sheet and alpha1-helix may affect the ligand-binding activity. The archetypical acetyltransferases AAPatAs possessing GNAT and ACT domains show a novel signaling pathway for regulating the acetylation of cellular proteins. The acetylation level of proteins may be closely correlated with intracellular concentrations of Asn and Cys in Actinobacteria
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physiological function
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lysine acetylation is a critical post-translational modification that influences protein activity, stability, and binding properties. The acetylation of histone proteins in particular is a feature of gene expression regulation. TgGCN5b is the only nuclear GCN5-family KAT known to be required for Toxoplasma tachyzoite replication
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physiological function
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GCN5-related N-acetyltransferases (GNATs) are a large and diverse group of enzymes which catalyze the transfer of an acetyl group from acetyl coenzyme A (Ac-CoA) to the amine group of a substrate. Substrates include protein N-terminus, lysine of histone tails, and other small molecules such as aminoglycoside, serotonin, and glucose-6-phosphate
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physiological function
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in Saccharomyces cerevisiae the lysine-acetyltransferase Gcn5 (KAT2) is part of the SAGA complex and is responsible for histone acetylation widely or at specific lysines. In wild-type mitochondria the Gcn5 protein is present in the mitoplasts, suggesting a distinct mitochondrial function for Gcn5 independent from the SAGA complex and possibly another function for this protein connecting epigenetics and metabolism, role of Gcn5 as a factor involved in respiratory metabolism, overview
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additional information
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development of a quantitative proteomic strategy to generate a comprehensive catalog of combinatorial histone acetylation and methylation motifs in Drosophila cells, acetylation patterns and their genesis by integrated enzyme activities, e.g. via enzymes MOF, RPD3, KAT6, NAA10, and GCN5, overview
additional information
mechanism by which GCN5b is recruited to target genes by co-purifying the enzyme with plant-like AP2-domain proteins, a subset of which function as DNA-binding transcription factors in Apicomplexa, overview
additional information
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mechanism by which GCN5b is recruited to target genes by co-purifying the enzyme with plant-like AP2-domain proteins, a subset of which function as DNA-binding transcription factors in Apicomplexa, overview
additional information
characterization of the Bacillus subtilis acetylome
additional information
in vitro-expressed full-length HBO1 exerts less acetylation activity compared to that of the separate MYST domain. The N-terminal domain may provide a regulatory switch for HBO1 activity
additional information
in vitro-expressed full-length HBO1 exerts less acetylation activity compared to that of the separate MYST domain. The N-terminal domain may provide a regulatory switch for HBO1 activity
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
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mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r)
additional information
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mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Rtt109 with bound acetyl-CoA (PDB ID 3qm0)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Rtt109 with bound acetyl-CoA (PDB ID 3qm0)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Rtt109 with bound acetyl-CoA (PDB ID 3qm0)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Rtt109 with bound acetyl-CoA (PDB ID 3qm0)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Rtt109 with bound acetyl-CoA (PDB ID 3qm0)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2)
additional information
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mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer
additional information
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mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs)
additional information
-
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs)
additional information
NuA4 is a 13-subunit KAT complex containing the essential catalytic domain Esa1 and held together by the scaffolding protein Eaf1
additional information
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NuA4 is a 13-subunit KAT complex containing the essential catalytic domain Esa1 and held together by the scaffolding protein Eaf1
additional information
screening of 544 human HAT-specific sites for acetylation by different HATs. Development the GPS 2.2 algorithm for the prediction of APC/C recognition motifs such as D-boxes and KEN-boxes proteins. The algorithm comprises two major parts, including the scoring strategy and performance improvement, method, overview
additional information
screening of 544 human HAT-specific sites for acetylation by different HATs. Development the GPS 2.2 algorithm for the prediction of APC/C recognition motifs such as D-boxes and KEN-boxes proteins. The algorithm comprises two major parts, including the scoring strategy and performance improvement, method, overview
additional information
screening of 544 human HAT-specific sites for acetylation by different HATs. Development the GPS 2.2 algorithm for the prediction of APC/C recognition motifs such as D-boxes and KEN-boxes proteins. The algorithm comprises two major parts, including the scoring strategy and performance improvement, method, overview
additional information
screening of 544 human HAT-specific sites for acetylation by different HATs. Development the GPS 2.2 algorithm for the prediction of APC/C recognition motifs such as D-boxes and KEN-boxes proteins. The algorithm comprises two major parts, including the scoring strategy and performance improvement, method, overview
additional information
screening of 544 human HAT-specific sites for acetylation by different HATs. Development the GPS 2.2 algorithm for the prediction of APC/C recognition motifs such as D-boxes and KEN-boxes proteins. The algorithm comprises two major parts, including the scoring strategy and performance improvement, method, overview
additional information
screening of 544 human HAT-specific sites for acetylation by different HATs. Development the GPS 2.2 algorithm for the prediction of APC/C recognition motifs such as D-boxes and KEN-boxes proteins. The algorithm comprises two major parts, including the scoring strategy and performance improvement, method, overview
additional information
screening of 544 human HAT-specific sites for acetylation by different HATs. Development the GPS 2.2 algorithm for the prediction of APC/C recognition motifs such as D-boxes and KEN-boxes proteins. The algorithm comprises two major parts, including the scoring strategy and performance improvement, method, overview
additional information
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screening of 544 human HAT-specific sites for acetylation by different HATs. Development the GPS 2.2 algorithm for the prediction of APC/C recognition motifs such as D-boxes and KEN-boxes proteins. The algorithm comprises two major parts, including the scoring strategy and performance improvement, method, overview
additional information
the enzyme contains an acetyl-CoA binding site located at the V-shaped cleft between beta4-beta5 strands created by beta-bulge on beta4. Another possible substrate binding site is identified close to the acetyl group of bound acetyl-CoA molecule. Acetyl-CoA adopts a C-shaped conformation where the adenosine diphosphate moiety is partly exposed to solvent and the acetyl group that is transferred to a substrate in a N-acetyltransferase reaction is deeply buried in the protein pointing towards a tunnel, potential substrate binding tunnel close to acetyl-CoA, overview. Structure comparisons
additional information
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the enzyme contains an acetyl-CoA binding site located at the V-shaped cleft between beta4-beta5 strands created by beta-bulge on beta4. Another possible substrate binding site is identified close to the acetyl group of bound acetyl-CoA molecule. Acetyl-CoA adopts a C-shaped conformation where the adenosine diphosphate moiety is partly exposed to solvent and the acetyl group that is transferred to a substrate in a N-acetyltransferase reaction is deeply buried in the protein pointing towards a tunnel, potential substrate binding tunnel close to acetyl-CoA, overview. Structure comparisons
additional information
the NAT activity is highest for the monomeric enzyme, about 2fold higher compared to the oligomeric enzyme and about 20% higher compared to the dimeric enzyme
additional information
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the NAT activity is highest for the monomeric enzyme, about 2fold higher compared to the oligomeric enzyme and about 20% higher compared to the dimeric enzyme
additional information
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the enzyme contains an acetyl-CoA binding site located at the V-shaped cleft between beta4-beta5 strands created by beta-bulge on beta4. Another possible substrate binding site is identified close to the acetyl group of bound acetyl-CoA molecule. Acetyl-CoA adopts a C-shaped conformation where the adenosine diphosphate moiety is partly exposed to solvent and the acetyl group that is transferred to a substrate in a N-acetyltransferase reaction is deeply buried in the protein pointing towards a tunnel, potential substrate binding tunnel close to acetyl-CoA, overview. Structure comparisons
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additional information
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characterization of the Bacillus subtilis acetylome
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additional information
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NuA4 is a 13-subunit KAT complex containing the essential catalytic domain Esa1 and held together by the scaffolding protein Eaf1
-
additional information
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the enzyme contains an acetyl-CoA binding site located at the V-shaped cleft between beta4-beta5 strands created by beta-bulge on beta4. Another possible substrate binding site is identified close to the acetyl group of bound acetyl-CoA molecule. Acetyl-CoA adopts a C-shaped conformation where the adenosine diphosphate moiety is partly exposed to solvent and the acetyl group that is transferred to a substrate in a N-acetyltransferase reaction is deeply buried in the protein pointing towards a tunnel, potential substrate binding tunnel close to acetyl-CoA, overview. Structure comparisons
-
additional information
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the enzyme contains an acetyl-CoA binding site located at the V-shaped cleft between beta4-beta5 strands created by beta-bulge on beta4. Another possible substrate binding site is identified close to the acetyl group of bound acetyl-CoA molecule. Acetyl-CoA adopts a C-shaped conformation where the adenosine diphosphate moiety is partly exposed to solvent and the acetyl group that is transferred to a substrate in a N-acetyltransferase reaction is deeply buried in the protein pointing towards a tunnel, potential substrate binding tunnel close to acetyl-CoA, overview. Structure comparisons
-
additional information
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the enzyme contains an acetyl-CoA binding site located at the V-shaped cleft between beta4-beta5 strands created by beta-bulge on beta4. Another possible substrate binding site is identified close to the acetyl group of bound acetyl-CoA molecule. Acetyl-CoA adopts a C-shaped conformation where the adenosine diphosphate moiety is partly exposed to solvent and the acetyl group that is transferred to a substrate in a N-acetyltransferase reaction is deeply buried in the protein pointing towards a tunnel, potential substrate binding tunnel close to acetyl-CoA, overview. Structure comparisons
-
additional information
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the enzyme contains an acetyl-CoA binding site located at the V-shaped cleft between beta4-beta5 strands created by beta-bulge on beta4. Another possible substrate binding site is identified close to the acetyl group of bound acetyl-CoA molecule. Acetyl-CoA adopts a C-shaped conformation where the adenosine diphosphate moiety is partly exposed to solvent and the acetyl group that is transferred to a substrate in a N-acetyltransferase reaction is deeply buried in the protein pointing towards a tunnel, potential substrate binding tunnel close to acetyl-CoA, overview. Structure comparisons
-
additional information
-
the enzyme contains an acetyl-CoA binding site located at the V-shaped cleft between beta4-beta5 strands created by beta-bulge on beta4. Another possible substrate binding site is identified close to the acetyl group of bound acetyl-CoA molecule. Acetyl-CoA adopts a C-shaped conformation where the adenosine diphosphate moiety is partly exposed to solvent and the acetyl group that is transferred to a substrate in a N-acetyltransferase reaction is deeply buried in the protein pointing towards a tunnel, potential substrate binding tunnel close to acetyl-CoA, overview. Structure comparisons
-
additional information
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mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
-
additional information
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mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Rtt109 with bound acetyl-CoA (PDB ID 3qm0)
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additional information
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the enzyme contains an acetyl-CoA binding site located at the V-shaped cleft between beta4-beta5 strands created by beta-bulge on beta4. Another possible substrate binding site is identified close to the acetyl group of bound acetyl-CoA molecule. Acetyl-CoA adopts a C-shaped conformation where the adenosine diphosphate moiety is partly exposed to solvent and the acetyl group that is transferred to a substrate in a N-acetyltransferase reaction is deeply buried in the protein pointing towards a tunnel, potential substrate binding tunnel close to acetyl-CoA, overview. Structure comparisons
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