compound induces hyperacetylation of specific lysine residues of histone H3, in particular residues K9 and K18, and raises the level of pan-acetylated H4. Compound inhibits the acetylation of all the other H3 and H4 lysines, with the exception of residue K8Ac of histone H4
Pat is a cAMP-regulated protein lysine acetyltransferase, that contains an additional nucleotide-binding domain that is structurally similar to the cAMP responsive region of protein kinase A, and inhibits acetyltransferase activity until cAMP is bound
compound induces hyperacetylation of specific lysine residues of histone H3, in particular residues K9 and K18, and raises the level of pan-acetylated H4
the transcription factor 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
after cytokine stimulation, IKKalpha also phosphorylates CBP at Ser1382 and Ser1386, thus enhancing CBP-binding affinity for p65 and CBP HAT activity and, consequently, histone H3 acetylation
laminar shear stress stimulates acetylation of histones 3 and 4 at the region of the eNOS promoter SSRE and extends 3' toward the eNOS coding region. Laminar shear stress induces p300 binding to p65 and leads to increase of p300 histone acetyltransferase activity by 2.5fold and to increase of acetylation of p65, but not of p50 acetylation, overview
p65-associated HAT activity. TNFalpha-dependent phosphorylation of p65 at either Ser276 or Ser536 increases its interaction with p300 and its subsequent acetylation at Lys310 of the NFkappaB subunit, indicating that p65 phosphorylation regulates subsequent acetylation
helper proteins required by Rtt109 for full catalytic activity. Stimulation of Rtt109 activity by Vps75 results in 50fold increase of the kcat value with unaltered Km
helper proteins required by Esa1 for full catalytic activity. Esa1 minimally requires Yng2 and Epl1 for full catalytic activity and nucleosome recognition
a short N-terminal region of BRPF2 (residues 31-80) is sufficient for binding to the enzyme and can potentiate its activity toward [histone H3]-L-lysine14
i.e. BRD1, BRPF2 is a cofactor directing HBO1 binding to the histone and binds to HBO1 in a cervical-loop structure proximity to the MYST domain to facilitate histone binding
i.e. BRD1, BRPF2 is a cofactor directing HBO1 binding to the histone and binds to HBO1 in a cervical-loop structure proximity to the MYST domain to facilitate histone binding. BRPF2 binds to HBO1 on the hinge connecting the NTD and MYST domain, thus it is reasonable to develop BRPF2-mimic peptides or molecules for disrupting HBO1-BRPF2 interaction andsubsequently prevent the binding of HBO1 to chromatin
ethanol induces the enzyme expression in the liver and activates the enzyme at specific lysine residues, e.g. Lys9 or Lys14, mechanisms of ethanol-induced histone H3 acetylation, overview
a significant induction of NF-kB p65-associated HAT activity by TNF-alpha is demonstrated, which is attenuated by the presence of montelukast in a concentration-dependent manner
Rtt109's H3-K9 acetylation activity in vitro is enhanced strongly by histone chaperone Vps75, Asf1, and Vps75 are both required for acetylation of Lys9 on H3 in vivo by Rtt109, whereas acetylation of Lys56 on H3 in vivo requires only Asf1
bombesin induces p300 expression 2fold, as part of the Src and PKCdelta pathways, a neutral endopeptidase, which degrades bombesin, or bombesin receptor antagonists, or p300 siRNA block bombesin-induced p300 HAT activity, overview
HATs form multisubunit complexes, and HAT interacting partners appear to regulate HAT activity by altering substrate specificity, targeting to specific loci, enhancing acetyltransferase activity, restricting access of non-target proteins, and coordinating the multiple enzyme activities of the complex
protein factors such as E1A and Nap1 can modulate p300/CBP HAT activity. Rtt109 requires a histone chaperone for efficient catalysis. HATs form multisubunit complexes, and HAT interacting partners appear to regulate HAT activity by altering substrate specificity, targeting to specific loci, enhancing acetyltransferase activity, restricting access of non-target proteins, and coordinating the multiple enzyme activities of the complex
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
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
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
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
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