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23S rRNA uridine2457
23S rRNA pseudouridine2457
human pre-tRNASer(UGA) uridine27
human pre-tRNASer(UGA) pseudouridine27
-
-
-
?
human tRNAMet uridine27
human tRNAMet pseudouridine27
-
-
-
?
KAR2 mRNA uridine
KAR2 mRNA pseudouridine
mitochondrial tRNAPhe uridine39
mitochondrial tRNAPhe pseudouridine39
-
-
-
?
mouse tRNAIle(UAU) uridine30
mouse tRNAIle(UAU) pseudouridine30
-
-
-
?
mouse tRNAMet uridine27
mouse tRNAMet pseudouridine27
-
-
-
?
pre-tRNAIle(UAU) uridine27
pre-tRNAIle(UAU) pseudouridine27
-
-
-
-
?
pre-tRNAIle(UAU) uridine30
pre-tRNAIle(UAU) pseudouridine30
-
-
-
-
?
pre-tRNAIle(UAU) uridine34
pre-tRNAIle(UAU) pseudouridine34
-
-
-
-
?
pre-tRNAIle(UAU) uridine36
pre-tRNAIle(UAU) pseudouridine36
-
-
-
-
?
RPL11a mRNA uridine68
RPL11a mRNA pseudouridine68
TEF1 mRNA uridine239
TEF1 mRNA pseudouridine239
tRNA uridine13
tRNA pseudouridine13
-
-
-
?
tRNAArg(ACG) uridine1
tRNAArg(ACG) pseudouridine1
tRNAIle uridine27
tRNAIle pseudouridine27
-
-
-
?
tRNAIle(UAU) uridine27
tRNAIle(UAU) pseudouridine27
tRNAIle(UAU) uridine34
tRNAIle(UAU) pseudouridine34
tRNAIle(UAU) uridine36
tRNAIle(UAU) pseudouridine36
tRNATrp(CCA) uridine26
tRNATrp(CCA) pseudouridine26
tRNATrp(CCA) uridine27
tRNATrp(CCA) pseudouridine27
tRNATrp(CCA) uridine28
tRNATrp(CCA) pseudouridine28
tRNATrp(CCA) uridine34
tRNATrp(CCA) pseudouridine34
-
-
-
?
tRNATrp(CCA) uridine35
tRNATrp(CCA) pseudouridine35
-
-
-
?
tRNATrp(CCA) uridine36
tRNATrp(CCA) pseudouridine36
-
-
-
?
tRNATrp(CCA) uridine65
tRNATrp(CCA) pseudouridine65
-
-
-
?
tRNATrp(CCA) uridine67
tRNATrp(CCA) pseudouridine67
-
-
-
?
tRNAVal uridine27
tRNAVal pseudouridine27
-
-
-
?
yeast pre-tRNAIle uridine
yeast pre-tRNAIle pseudouridine
possible modification sites are uridine 27, uridine30, uridine34 or uridine36
-
-
?
yeast tRNASer(UAU) uridine27
yeast tRNASer(UAU) pseudouridine27
-
-
-
?
yeast tRNASer(UAU) uridine34
yeast tRNASer(UAU) pseudouridine34
-
-
-
?
yeast tRNASer(UAU) uridine36
yeast tRNASer(UAU) pseudouridine36
-
-
-
?
yeast tRNAVal(UAC) uridine27
yeast tRNAVal(UAC) pseudouridine27
-
-
-
?
yeast tRNAVal(UAC) uridine32
yeast tRNAVal(UAC) pseudouridine32
-
-
-
?
additional information
?
-
23S rRNA uridine2457
23S rRNA pseudouridine2457
RluE forms a highly conserved pseudouridine during ribosome biogenesis
-
-
?
23S rRNA uridine2457
23S rRNA pseudouridine2457
RluE recognizes a large part of 23S rRNA comprising both H89 and the single-stranded flanking regions which explains the high substrate specificity of RluE
-
-
?
23S rRNA uridine2457
23S rRNA pseudouridine2457
RluE forms a highly conserved pseudouridine during ribosome biogenesis
-
-
?
KAR2 mRNA uridine
KAR2 mRNA pseudouridine
-
-
-
?
KAR2 mRNA uridine
KAR2 mRNA pseudouridine
-
-
-
?
RPL11a mRNA uridine68
RPL11a mRNA pseudouridine68
the Pus1 enzyme is necessary and sufficient for pseudouridylation of RPL11a mRNA
-
-
?
RPL11a mRNA uridine68
RPL11a mRNA pseudouridine68
the Pus1 enzyme is necessary and sufficient for pseudouridylation of RPL11a mRNA
-
-
?
TEF1 mRNA uridine239
TEF1 mRNA pseudouridine239
-
-
-
?
TEF1 mRNA uridine239
TEF1 mRNA pseudouridine239
-
-
-
?
tRNAArg(ACG) uridine1
tRNAArg(ACG) pseudouridine1
-
Pus1p can catalyze pseudouridine1 formation in the mature tRNAArg, the pre-tRNAArg, and its maturation intermediates
-
-
?
tRNAArg(ACG) uridine1
tRNAArg(ACG) pseudouridine1
Pus1p can catalyze pseudouridine1 formation in the mature tRNAArg, the pre-tRNAArg, and its maturation intermediates
-
-
?
tRNAIle(UAU) uridine27
tRNAIle(UAU) pseudouridine27
intron-independent reaction
-
-
?
tRNAIle(UAU) uridine27
tRNAIle(UAU) pseudouridine27
intron-independent reaction, reaction is catalyzed efficiently
-
-
?
tRNAIle(UAU) uridine34
tRNAIle(UAU) pseudouridine34
intron-dependent reaction
-
-
?
tRNAIle(UAU) uridine34
tRNAIle(UAU) pseudouridine34
reaction is strictly intron-dependent
-
-
?
tRNAIle(UAU) uridine36
tRNAIle(UAU) pseudouridine36
intron-dependent reaction
-
-
?
tRNAIle(UAU) uridine36
tRNAIle(UAU) pseudouridine36
reaction is strictly intron-dependent
-
-
?
tRNATrp(CCA) uridine26
tRNATrp(CCA) pseudouridine26
-
low activity
-
-
?
tRNATrp(CCA) uridine26
tRNATrp(CCA) pseudouridine26
-
-
-
?
tRNATrp(CCA) uridine27
tRNATrp(CCA) pseudouridine27
-
-
-
-
?
tRNATrp(CCA) uridine27
tRNATrp(CCA) pseudouridine27
-
-
-
?
tRNATrp(CCA) uridine28
tRNATrp(CCA) pseudouridine28
-
low activity
-
-
?
tRNATrp(CCA) uridine28
tRNATrp(CCA) pseudouridine28
-
-
-
?
tRNATrp(CCA) uridine28
tRNATrp(CCA) pseudouridine28
-
-
-
?
additional information
?
-
-
dual nature of pseudouridylation in U2 snRNA, Pus1p-dependent and Pus1p-independent activities. Pus1p from Caenorhabditis elegans has no enzymatic activity on U2 snRNA when expressed in yeast cells. Substrate specificity analysis and comparison of different species
-
-
?
additional information
?
-
-
dual nature of pseudouridylation in U2 snRNA, Pus1p-dependent and Pus1p-independent activities. Position 44 in yeast U2 snRNA (equivalent to position 43 in vertebrates) is a genuine substrate for Pus1p. Substrate specificity analysis and comparison of different species, two types of pseudouridine synthase that catalyze the formation of U2-?43 (or 44) in yeasts, Drosophila, and vertebrates
-
-
?
additional information
?
-
-
dual nature of pseudouridylation in U2 snRNA, Pus1p-dependent and Pus1p-independent activities. Position 44 in yeast U2 snRNA (equivalent to position 43 in vertebrates) is a genuine substrate for Pus1p. Substrate specificity analysis and comparison of different species, two types of pseudouridine synthase that catalyze the formation of U2-?43 (or 44) in yeasts, Drosophila, and vertebrates
-
-
?
additional information
?
-
Pus1p modifies uridines at positions 1, 26, 27, 28, 30, 34, 36, 65, and 67 depending on the source of the enzyme (Saccharomyces cerevisiae or mouse), the substrates (intron-containing or not), or whether the activity is monitored in vivo or in vitro. Out of all the positions that Pus1p modifies, the modification of uridines at positions 27 and 28 is by far the most common in tRNAs, with pseudouridine infrequently found at the other positions that the Pus1p enzymes recognize
-
-
?
additional information
?
-
-
Pus1p modifies uridines at positions 1, 26, 27, 28, 30, 34, 36, 65, and 67 depending on the source of the enzyme (Saccharomyces cerevisiae or mouse), the substrates (intron-containing or not), or whether the activity is monitored in vivo or in vitro. Out of all the positions that Pus1p modifies, the modification of uridines at positions 27 and 28 is by far the most common in tRNAs, with pseudouridine infrequently found at the other positions that the Pus1p enzymes recognize
-
-
?
additional information
?
-
pseudouridine synthase assays of hPus1p enzymes tRNA and HP7 SRA RNA substrates, i.e. RNA of the minimal RNA fragment within steroid receptor RNA activator (SRA), termed HP7. Mouse mitochondrial tRNAAsp is used as a positive control for hPus1p activity
-
-
?
additional information
?
-
-
pseudouridine synthase assays of hPus1p enzymes tRNA and HP7 SRA RNA substrates, i.e. RNA of the minimal RNA fragment within steroid receptor RNA activator (SRA), termed HP7. Mouse mitochondrial tRNAAsp is used as a positive control for hPus1p activity
-
-
?
additional information
?
-
-
does not pseudouridylate uridine30
-
-
?
additional information
?
-
-
dual nature of pseudouridylation in U2 snRNA, Pus1p-dependent and Pus1p-independent activities. Position 44 in yeast U2 snRNA (equivalent to position 43 in vertebrates) is a genuine substrate for Pus1p. In vertrbrates, SCARNA8 (also known as U92 scaRNA) is a guide for U2-Psi43 in addition to established targets U2-Psi34/Psi44. U2 snRNA is identified as a genuine substrate for mPus1p. Substrate specificity analysis and comparison of different species, two types of pseudouridine synthase that catalyze the formation of U2-Psi43 (or 44) in yeasts, Drosophila, and vertebrates
-
-
?
additional information
?
-
Pus1p catalyzes the formation of pseudouridines in several positions and in a number of different tRNA species
-
-
?
additional information
?
-
-
Pus1p catalyzes the formation of pseudouridines in several positions and in a number of different tRNA species
-
-
?
additional information
?
-
Pus1 from Saccharomyces cerevisiae is a multisite-specific enzyme that catalyses the formation of pseudouridine residues at different positions in several tRNA transcripts
-
-
?
additional information
?
-
for tRNA and Pus7, many known sites and their associated modifiers are identified, including Pus1-mediated Psi sites at positions 26-28 in several tRNAs, Pus7-dependent sites at position 13 of glutamate tRNA, Pus9-dependent site in mitochondrial aspartate tRNA at position 32, and Deg1-dependent sites at positions 37-38 in several tRNAs. Pseudouridylation in ncRNAs at sites of inter or intra-molecular interactions
-
-
?
additional information
?
-
-
Pus1p is the only pseudouridine synthase in Saccharomyces cerevisiae that is active on U2 snRNA at position 44. Yeast U2 snRNA is normally pseudouridylated at positions 35, 42, and 44
-
-
?
additional information
?
-
-
dual nature of pseudouridylation in U2 snRNA, Pus1p-dependent and Pus1p-independent activities. Position 44 in yeast U2 snRNA (equivalent to position 43 in vertebrates) is a genuine substrate for Pus1p. Besides U2 and U6 snRNAs in Saccharomyces cerevisiae, the enzyme modifies uridines in many different tRNAs. Substrate specificity analysis and comparison of different species, two types of pseudouridine synthase that catalyze the formation of U2-?43 (or 44) in yeasts, Drosophila, and vertebrates
-
-
?
additional information
?
-
-
Pus1p is the only pseudouridine synthase in Saccharomyces cerevisiae that is active on U2 snRNA at position 44. Yeast U2 snRNA is normally pseudouridylated at positions 35, 42, and 44
-
-
?
additional information
?
-
-
dual nature of pseudouridylation in U2 snRNA, Pus1p-dependent and Pus1p-independent activities. Position 44 in yeast U2 snRNA (equivalent to position 43 in vertebrates) is a genuine substrate for Pus1p. Besides U2 and U6 snRNAs in Saccharomyces cerevisiae, the enzyme modifies uridines in many different tRNAs. Substrate specificity analysis and comparison of different species, two types of pseudouridine synthase that catalyze the formation of U2-?43 (or 44) in yeasts, Drosophila, and vertebrates
-
-
?
additional information
?
-
-
dual nature of pseudouridylation in U2 snRNA, Pus1p-dependent and Pus1p-independent activities. Position 44 in yeast U2 snRNA (equivalent to position 43 in vertebrates) is a genuine substrate for Pus1p. Substrate specificity analysis and comparison of different species, two types of pseudouridine synthase that catalyze the formation of U2-Psi43 (or 44) in yeasts, Drosophila, and vertebrates
-
-
?
additional information
?
-
-
dual nature of pseudouridylation in U2 snRNA, Pus1p-dependent and Pus1p-independent activities. Position 44 in yeast U2 snRNA (equivalent to position 43 in vertebrates) is a genuine substrate for Pus1p. Substrate specificity analysis and comparison of different species, two types of pseudouridine synthase that catalyze the formation of U2-Psi43 (or 44) in yeasts, Drosophila, and vertebrates
-
-
?
additional information
?
-
extensive, regulated pseudouridylation of Toxoplasma mRNA with evidence for 1669 and 394 sites of pseudouridylation in tachyzoite and bradyzoite mRNAs, respectively. The distribution of Us and Psis is significantly different between the three regions of the transcript. Pseudouridylation is underrepresented in the 3'-UTR. At least in tachyzoites, TgPUS1-dependent Psis are distributed within the codon comparably toTgPUS1-independent Psis
-
-
?
additional information
?
-
-
extensive, regulated pseudouridylation of Toxoplasma mRNA with evidence for 1669 and 394 sites of pseudouridylation in tachyzoite and bradyzoite mRNAs, respectively. The distribution of Us and Psis is significantly different between the three regions of the transcript. Pseudouridylation is underrepresented in the 3'-UTR. At least in tachyzoites, TgPUS1-dependent Psis are distributed within the codon comparably toTgPUS1-independent Psis
-
-
?
additional information
?
-
identification of TgPUS1-dependent Psis in Toxoplasma RNA. Psis are relatively depleted in the 3'-UTR but enriched at position 1 of codons, identification by CMCT treatment combined with deep sequencing. Human rRNA data can be used to establish criteria for identification of Psis with high confidence, method evaluation, overview. PSI-seq identifies evolutionarily conserved sites of pseudouridylation in Toxoplasma gondii rRNAs. Determination of three TgPUS1-dependent Psis, all in the 5' half of the anticodon arm, specifically at positions 27 and 34 of tRNA Val and Asn (TGME49_251700 and TGME49_293750) in tachyzoites and position 28 of tRNA Ile (TGME49_262568) in bradyzoites
-
-
?
additional information
?
-
-
identification of TgPUS1-dependent Psis in Toxoplasma RNA. Psis are relatively depleted in the 3'-UTR but enriched at position 1 of codons, identification by CMCT treatment combined with deep sequencing. Human rRNA data can be used to establish criteria for identification of Psis with high confidence, method evaluation, overview. PSI-seq identifies evolutionarily conserved sites of pseudouridylation in Toxoplasma gondii rRNAs. Determination of three TgPUS1-dependent Psis, all in the 5' half of the anticodon arm, specifically at positions 27 and 34 of tRNA Val and Asn (TGME49_251700 and TGME49_293750) in tachyzoites and position 28 of tRNA Ile (TGME49_262568) in bradyzoites
-
-
?
additional information
?
-
-
dual nature of pseudouridylation in U2 snRNA, Pus1p-dependent and Pus1p-independent activities. Position 44 in yeast U2 snRNA (equivalent to position 43 in vertebrates) is a genuine substrate for Pus1p. In vertrbrates, SCARNA8 (also known as U92 scaRNA) is a guide for U2-Psi43 in addition to established targets U2-Psi34/Psi44. Substrate specificity analysis and comparison of different species, two types of pseudouridine synthase that catalyze the formation of U2-?43 (or 44) in yeasts, Drosophila, and vertebrates
-
-
?
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23S rRNA uridine2457
23S rRNA pseudouridine2457
KAR2 mRNA uridine
KAR2 mRNA pseudouridine
mitochondrial tRNAPhe uridine39
mitochondrial tRNAPhe pseudouridine39
-
-
-
?
RPL11a mRNA uridine68
RPL11a mRNA pseudouridine68
TEF1 mRNA uridine239
TEF1 mRNA pseudouridine239
tRNA uridine13
tRNA pseudouridine13
-
-
-
?
additional information
?
-
23S rRNA uridine2457
23S rRNA pseudouridine2457
RluE forms a highly conserved pseudouridine during ribosome biogenesis
-
-
?
23S rRNA uridine2457
23S rRNA pseudouridine2457
RluE forms a highly conserved pseudouridine during ribosome biogenesis
-
-
?
KAR2 mRNA uridine
KAR2 mRNA pseudouridine
-
-
-
?
KAR2 mRNA uridine
KAR2 mRNA pseudouridine
-
-
-
?
RPL11a mRNA uridine68
RPL11a mRNA pseudouridine68
the Pus1 enzyme is necessary and sufficient for pseudouridylation of RPL11a mRNA
-
-
?
RPL11a mRNA uridine68
RPL11a mRNA pseudouridine68
the Pus1 enzyme is necessary and sufficient for pseudouridylation of RPL11a mRNA
-
-
?
TEF1 mRNA uridine239
TEF1 mRNA pseudouridine239
-
-
-
?
TEF1 mRNA uridine239
TEF1 mRNA pseudouridine239
-
-
-
?
additional information
?
-
Pus1p catalyzes the formation of pseudouridines in several positions and in a number of different tRNA species
-
-
?
additional information
?
-
-
Pus1p catalyzes the formation of pseudouridines in several positions and in a number of different tRNA species
-
-
?
additional information
?
-
for tRNA and Pus7, many known sites and their associated modifiers are identified, including Pus1-mediated Psi sites at positions 26-28 in several tRNAs, Pus7-dependent sites at position 13 of glutamate tRNA, Pus9-dependent site in mitochondrial aspartate tRNA at position 32, and Deg1-dependent sites at positions 37-38 in several tRNAs. Pseudouridylation in ncRNAs at sites of inter or intra-molecular interactions
-
-
?
additional information
?
-
-
Pus1p is the only pseudouridine synthase in Saccharomyces cerevisiae that is active on U2 snRNA at position 44. Yeast U2 snRNA is normally pseudouridylated at positions 35, 42, and 44
-
-
?
additional information
?
-
-
Pus1p is the only pseudouridine synthase in Saccharomyces cerevisiae that is active on U2 snRNA at position 44. Yeast U2 snRNA is normally pseudouridylated at positions 35, 42, and 44
-
-
?
additional information
?
-
extensive, regulated pseudouridylation of Toxoplasma mRNA with evidence for 1669 and 394 sites of pseudouridylation in tachyzoite and bradyzoite mRNAs, respectively. The distribution of Us and Psis is significantly different between the three regions of the transcript. Pseudouridylation is underrepresented in the 3'-UTR. At least in tachyzoites, TgPUS1-dependent Psis are distributed within the codon comparably toTgPUS1-independent Psis
-
-
?
additional information
?
-
-
extensive, regulated pseudouridylation of Toxoplasma mRNA with evidence for 1669 and 394 sites of pseudouridylation in tachyzoite and bradyzoite mRNAs, respectively. The distribution of Us and Psis is significantly different between the three regions of the transcript. Pseudouridylation is underrepresented in the 3'-UTR. At least in tachyzoites, TgPUS1-dependent Psis are distributed within the codon comparably toTgPUS1-independent Psis
-
-
?
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evolution
eukaryal Pus10 genes share a conserved catalytic domain with archaeal Pus10 genes. Pus10 is found in earlier evolutionary branches of fungi (such as chytrid Batrachochytrium) but is absent in all dikaryon fungi surveyed (Ascomycetes and Basidiomycetes). Orthologs of Pus10, TrmA, and TruB are present in all the animals, plants, and protozoa surveyed. This indicates that the common eukaryotic ancestor possesses all the three genes. Pus10 exists as a single copy gene in all the surveyed genomes despite ancestral whole genome duplications has occurred. This indicates a possible deleterious gene dosage effect. Functional redundancy results in gene loss or neofunctionalization in different evolutionary lineages
evolution
eukaryal Pus10 genes share a conserved catalytic domain with archaeal Pus10 genes. Pus10 is found in earlier evolutionary branches of fungi (such as chytrid Batrachochytrium) but is absent in all dikaryon fungi surveyed (Ascomycetes and Basidiomycetes). Orthologs of Pus10, TrmA, and TruB are present in all the animals, plants, and protozoa surveyed. This indicates that the common eukaryotic ancestor possesses all the three genes. Pus10 exists as a single copy gene in all the surveyed genomes despite ancestral whole genome duplications has occurred. This indicates a possible deleterious gene dosage effect. Functional redundancy results in gene loss or neofunctionalization in different evolutionary lineages
evolution
eukaryal Pus10 genes share a conserved catalytic domain with archaeal Pus10 genes. Pus10 is found in earlier evolutionary branches of fungi (such as chytrid Batrachochytrium) but is absent in all dikaryon fungi surveyed (Ascomycetes and Basidiomycetes). Orthologs of Pus10, TrmA, and TruB are present in all the animals, plants, and protozoa surveyed. This indicates that the common eukaryotic ancestor possesses all the three genes. Pus10 exists as a single copy gene in all the surveyed genomes despite ancestral whole genome duplications has occurred. This indicates a possible deleterious gene dosage effect. Functional redundancy results in gene loss or neofunctionalization in different evolutionary lineages
evolution
eukaryal Pus10 genes share a conserved catalytic domain with archaeal Pus10 genes. Pus10 is found in earlier evolutionary branches of fungi (such as chytrid Batrachochytrium) but is absent in all dikaryon fungi surveyed (Ascomycetes and Basidiomycetes). Orthologs of Pus10, TrmA, and TruB are present in all the animals, plants, and protozoa surveyed. This indicates that the common eukaryotic ancestor possesses all the three genes. Pus10 exists as a single copy gene in all the surveyed genomes despite ancestral whole genome duplications has occurred. This indicates a possible deleterious gene dosage effect. Functional redundancy results in gene loss or neofunctionalization in different evolutionary lineages
evolution
-
Pus1p is a member of the TruA pseudouridine synthase family
evolution
-
Pus1p is a member of the TruA pseudouridine synthase family
evolution
-
Pus1p is a member of the TruA pseudouridine synthase family
evolution
-
Pus1p is a member of the TruA pseudouridine synthase family
evolution
-
Pus1p is a member of the TruA pseudouridine synthase family
evolution
-
Pus1p is a member of the TruA pseudouridine synthase family
evolution
-
Pus1p is a member of the TruA pseudouridine synthase family
-
evolution
-
Pus1p is a member of the TruA pseudouridine synthase family
-
evolution
-
Pus1p is a member of the TruA pseudouridine synthase family
-
malfunction
missense mutation in PUS1 causes mitochondrial myopathy and sideroblastic anemia (a rare, autosomal recessive oxidative phosphorylation disorder specific to skeletal muscle and bone marrow)
malfunction
the disruption of the Pus1 gene confers no obvious phenotype
malfunction
depletion of RPUSD4 leads to a severe reduction of the steady-state level of the 16S mitochondrial rRNA with defects in the biogenesis of the mitoribosome large subunit and consequently in mitochondrial translation
malfunction
-
in mutant worms, the absence of Pus1p activity on tRNAs has no effect on U2 snRNA modification
malfunction
PUS1 gene disruption mutants of Toxoplasma gondii are defective in differentiation from tachyzoites to bradyzoites. Pseudouridylation of the 5'-UTR and coding regions has a modest effect on steady-state mRNA levels, and the mRNA stability is modestly affected by TgPUS1-dependent pseudouridylation
malfunction
-
U2 snRNAs from Pus1 knockout mice show no changes in their modification patterns when compared to wild-type U2 snRNAs. In Pus1-knockout mice, Pus1p-dependent modification of tRNAs is missing. No differences between wild-type and mutant mice in their U2 snRNA modification patterns
malfunction
-
U2 snRNAs from pus1DELTA Schizosaccharomyces pombe knockout strain show no changes in their modification patterns when compared to wild-type U2 snRNAs. A novel box H/ACA RNA is found encoded downstream from the RPC10 gene and experimentally verified its guide RNA activity for positioning Psi43 and Psi44 in U2 snRNA
malfunction
-
U2 snRNAs from pus1DELTA Schizosaccharomyces pombe knockout strain show no changes in their modification patterns when compared to wild-type U2 snRNAs. A novel box H/ACA RNA is found encoded downstream from the RPC10 gene and experimentally verified its guide RNA activity for positioning Psi43 and Psi44 in U2 snRNA
-
metabolism
human Pus10 participates in apoptosis induced by the tumor necrosis factor-related apoptosis-inducing ligand
metabolism
pseudouridine synthase RPUSD4 is an essential component of mitochondrial RNA granules. Several steps of mitochondrial RNA processing and maturation, including RNA post-transcriptional modification, are spatially organized into mitochondrial RNA granules
metabolism
RluE is a faster pseudouridine synthase than other enzymes which likely enables it to act in the early stages of ribosome form
metabolism
the enzyme is required for proper chloroplast rRNA processing and protein translation
metabolism
the enzyme modulate class I and class II nuclear receptor responses through its ability to modify the steroid receptor RNA activator
metabolism
the Pus1 enzyme is necessary and sufficient for pseudouridylation of RPL11a mRNA
metabolism
-
the Pus1 enzyme is necessary and sufficient for pseudouridylation of RPL11a mRNA
-
metabolism
-
RluE is a faster pseudouridine synthase than other enzymes which likely enables it to act in the early stages of ribosome form
-
physiological function
a pseudouridine synthase (TgPUS1) is necessary for differentiation of the single celled eukaryotic parasite Toxoplasma gondii from active to chronic infection. Many Psis in tRNA and mRNA are dependent on the action of TgPUS1, and TgPUS1-dependent mRNA Psis are enriched in developmentally regulated transcripts. Genes containing a TgPUS1-dependent Psi are relatively more abundant in mutant parasites, mRNAs containing TgPUS1-dependent Psi have a modest but statistically significant increase in half-life in the mutant parasites. mRNA Psis play an important biological role. PUS is necessary for differentiation of the parasite Toxoplasma gondii. Pseudouridylation of spliceosomal RNAs is TgPUS1-independent
physiological function
-
in vertebrate SCARNA8, stronger binding in the alternative configuration to position U2-Psi45 might facilitate efficient sliding to position U2-Psi44. Multiple guide RNAs are typically assigned to the most important modified positions. Pseudouridines at the branch point recognition region of U2 snRNA represent such functionally crucial modifications
physiological function
-
in vertebrate SCARNA8, stronger binding in the alternative configuration to position U2-Psi45 might facilitate efficient sliding to position U2-Psi44. Multiple guide RNAs are typically assigned to the most important modified positions. Pseudouridines at the branch point recognition region of U2 snRNA represent such functionally crucial modifications
physiological function
-
multiple guide RNAs are typically assigned to the most important modified positions. Pseudouridines at the branch point recognition region of U2 snRNA represent such functionally crucial modifications
physiological function
-
multiple guide RNAs are typically assigned to the most important modified positions. Pseudouridines at the branch point recognition region of U2 snRNA represent such functionally crucial modifications
physiological function
-
multiple guide RNAs are typically assigned to the most important modified positions. Pseudouridines at the branch point recognition region of U2 snRNA represent such functionally crucial modifications
physiological function
-
multiple guide RNAs are typically assigned to the most important modified positions. Pseudouridines at the branch point recognition region of U2 snRNA represent such functionally crucial modifications
physiological function
the most abundant RNA modification is pseudouridine (Psi), Psi is ubiquitous in diverse RNAs, and dynamic in mRNA. Pseudouridylation profiles and mechanisms. Pus7-dependent induction of pseudouridylation during heat shock
physiological function
-
multiple guide RNAs are typically assigned to the most important modified positions. Pseudouridines at the branch point recognition region of U2 snRNA represent such functionally crucial modifications
-
physiological function
-
multiple guide RNAs are typically assigned to the most important modified positions. Pseudouridines at the branch point recognition region of U2 snRNA represent such functionally crucial modifications
-
physiological function
-
multiple guide RNAs are typically assigned to the most important modified positions. Pseudouridines at the branch point recognition region of U2 snRNA represent such functionally crucial modifications
-
additional information
hPus1p active site architecture analysis, overview
additional information
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hPus1p active site architecture analysis, overview
additional information
pseudouridines in Toxoplasma snRNAs are homologous to those in Saccharomyces cerevisiae and human snRNAs, and are not TgPUS1-dependent
additional information
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pseudouridines in Toxoplasma snRNAs are homologous to those in Saccharomyces cerevisiae and human snRNAs, and are not TgPUS1-dependent
additional information
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screening for other potential guide RNAs for pseudouridylation of position 43 in U2 snRNA, vertebrate box H/ACA RNAs for antisense elements specific to the U2 snRNA branch point recognition region. The SNORA71 5'-terminal pseudouridylation pocket can base pair with U2 snRNA, both positions 43 and 41 can be modified by base-pairing within the same pseudouridylation pocket
additional information
-
screening for other potential guide RNAs for pseudouridylation of position 43 in U2 snRNA, vertebrate box H/ACA RNAs for antisense elements specific to the U2 snRNA branch point recognition region. The SNORA71 5'-terminal pseudouridylation pocket can base pair with U2 snRNA, both positions 43 and 41 can be modified by base-pairing within the same pseudouridylation pocket
additional information
transcriptome-wide quantitative mapping of Psi, method development using Psi-seq, relying on the unique stability of N3-[N-cyclohexyl-N'-beta-(4-methylmorpholinium)ethylcarbodiimide-Psi] (N3-CMC-Psi) to alkaline hydrolysis, and the ability of N3-CMC-Psi to terminate reverse transcription. For rRNA, 24/24 Cbf5-dependent sites are known targets of pseudouridylation, 8/9 associations between snoRNAs and rRNA sites are known, as is the identified Pus5-mediated Psi site in mitochondrial 21S rRNA. One snR3-dependent site at position 2140 on 25S rRNA is not specificated, detailed overview. Cbf5-dependent Psi sites in mRNAs and snoRNAs are likely snoRNA-guided
additional information
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U2 snRNA can be modified in Caenorhabditis elegans by a Pus1p-independent mechanism
additional information
-
U2 snRNA can be modified in Schizosaccharomyces pombe by a Pus1p-independent mechanism
additional information
-
U2 snRNA can be modified in Schizosaccharomyces pombe by a Pus1p-independent mechanism
-
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D146A
site-directed mutagenesis of truncated enzyme mutant DELTAhPus1p, differences between structures of DELTAhPus1p and DELTAhPus1pD146A are limited to external, poorly conserved loops, which confirm the flexibility of these regions
R116A
the mutant exhibits some activity with the yeast pre-tRNAIle substrate. Low activity with the mouse tRNAMet substrate
R116C
the activity of the mutant enzyme with the yeast pre-tRNAIle substrate is approximately one-third that of the wild-type levels. No activity with the mouse tRNAMet substrate
R116E
the mutant is inactive with with the yeast pre-tRNAIle substrate. No activity with the mouse tRNAMet substrate
R116G
the mutant exhibits some activity with the yeast pre-tRNAIle substrate. No activity with the mouse tRNAMet substrate
R116H
the mutant is inactive with with the yeast pre-tRNAIle substrate. Low activity with the mouse tRNAMet substrate
R116K
the activity of the mutant enzyme with the yeast pre-tRNAIle substrate is approximately one-third that of the wild-type levels
R116N
the mutant exhibits some activity with the yeast pre-tRNAIle substrate. No activity with the mouse tRNAMet substrate
R116Q
the mutant exhibits some activity with the yeast pre-tRNAIle substrate. No activity with the mouse tRNAMet substrate
R116S
the mutant exhibits some activity with the yeast pre-tRNAIle substrate. No activity with the mouse tRNAMet substrate
R116W
the mutant is inactive with with the yeast pre-tRNAIle substrate. Low activity with the mouse tRNAMet substrate
Y173C
mutant enzyme retains some activity with yeast pre-tRNAIle. The activity is relatively low
Y173G
mutant enzyme retains some activity with yeast pre-tRNAIle. The activity is relatively low
Y173S
mutant enzyme is minimally activity with yeast pre-tRNAIle
D112A
-
inactive mutant enzyme
Y173F
mutant enzyme is minimally activity with yeast pre-tRNAIle
Y173F
mutant enzyme retains some activity with yeast pre-tRNAIle. The activity is relatively low
Y173T
mutant enzyme is minimally activity with yeast pre-tRNAIle
Y173T
mutant enzyme retains some activity with yeast pre-tRNAIle. The activity is relatively low
additional information
generation of a truncated hPus1p version encompassing residues 83-394, i.e. DELTAhPus1p. The deleted N- and C-termini are not essential for either the RNA binding or the activity of the hPus1p enzyme
additional information
-
generation of a truncated hPus1p version encompassing residues 83-394, i.e. DELTAhPus1p. The deleted N- and C-termini are not essential for either the RNA binding or the activity of the hPus1p enzyme
additional information
-
generation of Pus1 knockout mice
additional information
-
generation of gene deletion mutant DELTApus1. which shows a U2 snRNA modification pattern identical to its parental wild-type strain ED666
additional information
-
generation of gene deletion mutant DELTApus1. which shows a U2 snRNA modification pattern identical to its parental wild-type strain ED666
-
additional information
-
SNORA71 is expressed in an enzyme knockout mutant yeast strain, but do not restore pseudouridylation of the endogenous yeast U2 snRNA
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Cloning and characterization of a mammalian pseudouridine synthase
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74
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A previously unidentified activity of yeast and mouse RNA:pseudouridine synthases 1 (Pus1p) on tRNAs
RNA
12
1583-1593
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Mus musculus, Saccharomyces cerevisiae (Q12211), Saccharomyces cerevisiae
brenda
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Partial activity is seen with many substitutions of highly conserved active site residues in human Pseudouridine synthase 1
RNA
14
1895-1906
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Homo sapiens (Q9Y606), Homo sapiens
brenda
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15
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1996
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brenda
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Cloning and characterization of the Schizosaccharomyces pombe tRNA:pseudouridine synthase Pus1p
Nucleic Acids Res.
28
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Schizosaccharomyces pombe (O94396), Schizosaccharomyces pombe
brenda
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Transcriptome-wide mapping reveals widespread dynamic-regulated pseudouridylation of ncRNA and mRNA
Cell
159
148-162
2014
Saccharomyces cerevisiae (Q08647)
brenda
Lu, S.; Li, C.; Zhang, Y.; Zheng, Z.; Liu, D.
Functional disruption of a chloroplast pseudouridine synthase desensitizes Arabidopsis plants to phosphate starvation
Front. Plant Sci.
8
1421
2017
Arabidopsis thaliana (Q8L960)
brenda
Zaganelli, S.; Rebelo-Guiomar, P.; Maundrell, K.; Rozanska, A.; Pierredon, S.; Powell, C.A.; Jourdain, A.A.; Hulo, N.; Lightowlers, R.N.; Chrzanowska-Lightowlers, Z.M.; Minczuk, M.; Martinou, J.C.
The pseudouridine synthase RPUSD4 is an essential component of mitochondrial RNA granules
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292
4519-4532
2017
Homo sapiens (Q96CM3)
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430
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2018
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Evolution of eukaryal and archaeal pseudouridine synthase Pus10
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86
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Arabidopsis thaliana (F4HSS8), Homo sapiens (Q3MIT2), Methanocaldococcus jannaschii (Q60346), Pyrococcus furiosus (Q8U1R6)
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Transcriptome-wide mapping of pseudouridines pseudouridine synthases modify specific mRNAs in S. cerevisiae
PLoS ONE
9
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Steroid receptor RNA activator (SRA) modification by the human pseudouridine synthase 1 (hPus1p) RNA binding, activity, and atomic model
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9
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Dual nature of pseudouridylation in U2 snRNA Pus1p-dependent and Pus1p-independent activities in yeasts and higher eukaryotes
RNA
23
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RNA
23
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