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Information on EC 5.4.99.B22 - multisite-specific tRNA pseudouridine synthase
for references in articles please use BRENDA:EC5.4.99.B22
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preliminary BRENDA-supplied EC number
EC Tree 5 Isomerases
5.4 Intramolecular transferases
5.4.99 Transferring other groups
5.4.99.B22 multisite-specific tRNA pseudouridine synthase
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
- 5.4.99.B22
-
pseudouridylation
- anemia
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sideroblastic
- myopathy
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dyskerin
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anticodon
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mlasa
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spliceosomal
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nuclear-encoded
- agriculture
Reaction Schemes
showtRNA uridine65
=
tRNA pseudouridine65
tRNA uridine26
=
tRNA pseudouridine26
tRNA uridine27
=
tRNA pseudouridine27
tRNA uridine28
=
tRNA pseudouridine28
tRNA uridine30
=
tRNA pseudouridine30
tRNA uridine34
=
tRNA pseudouridine34
tRNA uridine35
=
tRNA pseudouridine35
tRNA uridine36
=
tRNA pseudouridine36
tRNA uridine67
=
tRNA pseudouridine67
Synonyms
pus1p, mpus1p, pseudouridine synthase 1, rpusd4, hpus1p, scpus1p, sppus1p, tgpus1, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dmPus1p
mPus1p
pseudouridine synthase Pus10
PUS1
Pus1p
Pus4
PUS6
RluE
RNA:pseudouridine synthases 1
spPus1p
YmfC
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
tRNA uridine26 = tRNA pseudouridine26
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tRNA uridine27 = tRNA pseudouridine27
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tRNA uridine28 = tRNA pseudouridine28
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tRNA uridine30 = tRNA pseudouridine30
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tRNA uridine34 = tRNA pseudouridine34
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tRNA uridine35 = tRNA pseudouridine35
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tRNA uridine36 = tRNA pseudouridine36
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tRNA uridine65 = tRNA pseudouridine65
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tRNA uridine67 = tRNA pseudouridine67
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SYSTEMATIC NAME
IUBMB Comments
multisite-specific tRNA-uridine uracil mutase
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
human pre-tRNASer(UGA) uridine27
human pre-tRNASer(UGA) pseudouridine27
Substrates: -
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?
human tRNAMet uridine27
human tRNAMet pseudouridine27
Substrates: -
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?
mitochondrial tRNAPhe uridine39
mitochondrial tRNAPhe pseudouridine39
Substrates: -
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?
mouse tRNAIle(UAU) uridine30
mouse tRNAIle(UAU) pseudouridine30
Substrates: -
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?
mouse tRNAMet uridine27
mouse tRNAMet pseudouridine27
Substrates: -
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?
pre-tRNAIle(UAU) uridine27
pre-tRNAIle(UAU) pseudouridine27
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Substrates: -
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?
pre-tRNAIle(UAU) uridine30
pre-tRNAIle(UAU) pseudouridine30
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Substrates: -
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?
pre-tRNAIle(UAU) uridine34
pre-tRNAIle(UAU) pseudouridine34
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Substrates: -
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?
pre-tRNAIle(UAU) uridine36
pre-tRNAIle(UAU) pseudouridine36
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Substrates: -
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?
tRNA uridine13
tRNA pseudouridine13
Substrates: -
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?
tRNAIle uridine27
tRNAIle pseudouridine27
Substrates: -
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?
tRNATrp(CCA) uridine34
tRNATrp(CCA) pseudouridine34
Substrates: -
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?
tRNATrp(CCA) uridine35
tRNATrp(CCA) pseudouridine35
Substrates: -
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?
tRNATrp(CCA) uridine36
tRNATrp(CCA) pseudouridine36
Substrates: -
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?
tRNATrp(CCA) uridine65
tRNATrp(CCA) pseudouridine65
Substrates: -
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?
tRNATrp(CCA) uridine67
tRNATrp(CCA) pseudouridine67
Substrates: -
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?
tRNAVal uridine27
tRNAVal pseudouridine27
Substrates: -
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?
yeast pre-tRNAIle uridine
yeast pre-tRNAIle pseudouridine
Substrates: possible modification sites are uridine 27, uridine30, uridine34 or uridine36
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?
yeast tRNASer(UAU) uridine27
yeast tRNASer(UAU) pseudouridine27
Substrates: -
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?
yeast tRNASer(UAU) uridine34
yeast tRNASer(UAU) pseudouridine34
Substrates: -
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?
yeast tRNASer(UAU) uridine36
yeast tRNASer(UAU) pseudouridine36
Substrates: -
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?
yeast tRNAVal(UAC) uridine27
yeast tRNAVal(UAC) pseudouridine27
Substrates: -
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?
yeast tRNAVal(UAC) uridine32
yeast tRNAVal(UAC) pseudouridine32
Substrates: -
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?
23S rRNA uridine2457
23S rRNA pseudouridine2457
Substrates: RluE forms a highly conserved pseudouridine during ribosome biogenesis
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?
23S rRNA uridine2457
23S rRNA pseudouridine2457
Substrates: 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
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?
23S rRNA uridine2457
23S rRNA pseudouridine2457
Substrates: RluE forms a highly conserved pseudouridine during ribosome biogenesis
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?
KAR2 mRNA uridine
KAR2 mRNA pseudouridine
Substrates: -
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?
KAR2 mRNA uridine
KAR2 mRNA pseudouridine
Substrates: -
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?
RPL11a mRNA uridine68
RPL11a mRNA pseudouridine68
Substrates: the Pus1 enzyme is necessary and sufficient for pseudouridylation of RPL11a mRNA
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?
RPL11a mRNA uridine68
RPL11a mRNA pseudouridine68
Substrates: the Pus1 enzyme is necessary and sufficient for pseudouridylation of RPL11a mRNA
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?
TEF1 mRNA uridine239
TEF1 mRNA pseudouridine239
Substrates: -
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?
TEF1 mRNA uridine239
TEF1 mRNA pseudouridine239
Substrates: -
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?
tRNAArg(ACG) uridine1
tRNAArg(ACG) pseudouridine1
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Substrates: Pus1p can catalyze pseudouridine1 formation in the mature tRNAArg, the pre-tRNAArg, and its maturation intermediates
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?
tRNAArg(ACG) uridine1
tRNAArg(ACG) pseudouridine1
Substrates: Pus1p can catalyze pseudouridine1 formation in the mature tRNAArg, the pre-tRNAArg, and its maturation intermediates
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?
tRNAIle(UAU) uridine27
tRNAIle(UAU) pseudouridine27
Substrates: intron-independent reaction
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?
tRNAIle(UAU) uridine27
tRNAIle(UAU) pseudouridine27
Substrates: intron-independent reaction, reaction is catalyzed efficiently
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?
tRNAIle(UAU) uridine34
tRNAIle(UAU) pseudouridine34
Substrates: reaction is strictly intron-dependent
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?
tRNAIle(UAU) uridine34
tRNAIle(UAU) pseudouridine34
Substrates: intron-dependent reaction
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?
tRNAIle(UAU) uridine36
tRNAIle(UAU) pseudouridine36
Substrates: reaction is strictly intron-dependent
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?
tRNAIle(UAU) uridine36
tRNAIle(UAU) pseudouridine36
Substrates: intron-dependent reaction
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?
tRNATrp(CCA) uridine26
tRNATrp(CCA) pseudouridine26
-
Substrates: low activity
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?
tRNATrp(CCA) uridine26
tRNATrp(CCA) pseudouridine26
Substrates: -
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?
tRNATrp(CCA) uridine27
tRNATrp(CCA) pseudouridine27
-
Substrates: -
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?
tRNATrp(CCA) uridine27
tRNATrp(CCA) pseudouridine27
Substrates: -
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?
tRNATrp(CCA) uridine28
tRNATrp(CCA) pseudouridine28
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Substrates: low activity
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?
tRNATrp(CCA) uridine28
tRNATrp(CCA) pseudouridine28
Substrates: -
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?
tRNATrp(CCA) uridine28
tRNATrp(CCA) pseudouridine28
Substrates: -
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additional information
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Substrates: 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
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additional information
?
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: does not pseudouridylate uridine30
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additional information
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Substrates: 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
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additional information
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Substrates: Pus1p catalyzes the formation of pseudouridines in several positions and in a number of different tRNA species
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additional information
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Substrates: Pus1p catalyzes the formation of pseudouridines in several positions and in a number of different tRNA species
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additional information
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Substrates: Pus1 from Saccharomyces cerevisiae is a multisite-specific enzyme that catalyses the formation of pseudouridine residues at different positions in several tRNA transcripts
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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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additional information
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Substrates: 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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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
mitochondrial tRNAPhe uridine39
mitochondrial tRNAPhe pseudouridine39
Substrates: -
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tRNA uridine13
tRNA pseudouridine13
Substrates: -
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23S rRNA uridine2457
23S rRNA pseudouridine2457
Substrates: RluE forms a highly conserved pseudouridine during ribosome biogenesis
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?
23S rRNA uridine2457
23S rRNA pseudouridine2457
Substrates: RluE forms a highly conserved pseudouridine during ribosome biogenesis
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?
KAR2 mRNA uridine
KAR2 mRNA pseudouridine
Substrates: -
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?
KAR2 mRNA uridine
KAR2 mRNA pseudouridine
Substrates: -
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?
RPL11a mRNA uridine68
RPL11a mRNA pseudouridine68
Substrates: the Pus1 enzyme is necessary and sufficient for pseudouridylation of RPL11a mRNA
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RPL11a mRNA uridine68
RPL11a mRNA pseudouridine68
Substrates: the Pus1 enzyme is necessary and sufficient for pseudouridylation of RPL11a mRNA
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?
TEF1 mRNA uridine239
TEF1 mRNA pseudouridine239
Substrates: -
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?
TEF1 mRNA uridine239
TEF1 mRNA pseudouridine239
Substrates: -
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additional information
?
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Substrates: Pus1p catalyzes the formation of pseudouridines in several positions and in a number of different tRNA species
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additional information
?
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Substrates: Pus1p catalyzes the formation of pseudouridines in several positions and in a number of different tRNA species
Products: -
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?
additional information
?
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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?
additional information
?
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Substrates: 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
Products: -
Products: -
?
additional information
?
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Substrates: 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
Products: -
Products: -
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KCl
the complex of Pus1 with tRNA is sensitive to high ionic strength. The optimal concentration of KCl for Pus1 binding is 100 mM. Above 400 mM KCl, no complex is detected
Zinc
contains one atom of zinc per 63000 Da monomer. This zinc ion could not be removed by treatment with EDTA or urea. However, a zinc-depleted enzyme is obtained after prolonged dialysis against the specific chelating agent 1,10-phenanthroline. Removal of the zinc ion results in inactivation of the enzyme with concomitant loss of its ability to bind tRNA. Structural role for the zinc in the tRNA-pseudouridine synthetase Pus1
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
the complex Pus1/tRNAVal is sensitive to the presence of EDTA
KCl
the complex of Pus1 with tRNA is sensitive to high ionic strength. The optimal concentration of KCl for Pus1 binding is 100 mM. Above 400 mM KCl, no complex is detected
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Anemia, Sideroblastic
Missense mutation in pseudouridine synthase 1 (PUS1) causes mitochondrial myopathy and sideroblastic anemia (MLASA).
Anemia, Sideroblastic
Mitochondrial myopathy and sideroblastic anemia (MLASA): missense mutation in the pseudouridine synthase 1 (PUS1) gene is associated with the loss of tRNA pseudouridylation.
Anemia, Sideroblastic
Pseudouridine synthase 1 deficient mice, a model for Mitochondrial Myopathy with Sideroblastic Anemia, exhibit muscle morphology and physiology alterations.
Anemia, Sideroblastic
Pus3p- and Pus1p-dependent pseudouridylation of steroid receptor RNA activator controls a functional switch that regulates nuclear receptor signaling.
Breast Neoplasms
The nucleolar-related protein Dyskerin pseudouridine synthase 1 (DKC1) predicts poor prognosis in breast cancer.
Colorectal Neoplasms
Dual Inhibition of DKC1 and MEK1/2 Synergistically Restrains the Growth of Colorectal Cancer Cells.
Dyskeratosis Congenita
Dyskeratosis congenita with a novel genetic variant in the DKC1 gene: a case report.
Mitochondrial Myopathies
Missense mutation in pseudouridine synthase 1 (PUS1) causes mitochondrial myopathy and sideroblastic anemia (MLASA).
Mitochondrial Myopathies
Mitochondrial myopathy and sideroblastic anemia (MLASA): missense mutation in the pseudouridine synthase 1 (PUS1) gene is associated with the loss of tRNA pseudouridylation.
Mitochondrial Myopathies
Pseudouridine synthase 1 deficient mice, a model for Mitochondrial Myopathy with Sideroblastic Anemia, exhibit muscle morphology and physiology alterations.
Mitochondrial Myopathies
Pus3p- and Pus1p-dependent pseudouridylation of steroid receptor RNA activator controls a functional switch that regulates nuclear receptor signaling.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00074
tRNAIle uridine27
pH and temperature not specified in the publication
-
0.00042
tRNAVal uridine27
pH and temperature not specified in the publication
-
0.000032
yeast pre-tRNAIle uridine
possible modification sites are uridine 27, uridine30, uridine34 or uridine36, wild-type enzyme, pH and temperature not specified in the publication
-
0.000168
yeast pre-tRNAIle uridine
possible modification sites are uridine 27, uridine30, uridine34 or uridine36, mutant enzyme R116K, pH and temperature not specified in the publication
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0083
tRNAIle uridine27
pH and temperature not specified in the publication
-
0.0067
tRNAVal uridine27
pH and temperature not specified in the publication
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11.26
tRNAIle uridine27
pH and temperature not specified in the publication
-
15.95
tRNAVal uridine27
pH and temperature not specified in the publication
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
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
-
malfunction
the disruption of the Pus1 gene confers no obvious phenotype
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
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
-
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
-
in mutant worms, the absence of Pus1p activity on tRNAs has no effect on U2 snRNA modification
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
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 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
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
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
human Pus10 participates in apoptosis induced by the tumor necrosis factor-related apoptosis-inducing ligand
metabolism
the enzyme is required for proper chloroplast rRNA processing and protein translation
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
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
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
-
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
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
-
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
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
hPus1p active site architecture analysis, overview
additional information
-
U2 snRNA can be modified in Schizosaccharomyces pombe by a Pus1p-independent mechanism
additional information
-
U2 snRNA can be modified in Caenorhabditis elegans by a Pus1p-independent mechanism
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
-
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
pseudouridines in Toxoplasma snRNAs are homologous to those in Saccharomyces cerevisiae and human snRNAs, and are not TgPUS1-dependent
additional information
-
pseudouridines in Toxoplasma snRNAs are homologous to those in Saccharomyces cerevisiae and human snRNAs, and are not TgPUS1-dependent
additional information
-
U2 snRNA can be modified in Schizosaccharomyces pombe by a Pus1p-independent mechanism
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PUS1_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
534
0
60324
Swiss-Prot
other Location (Reliability: 1)
PUS4_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
403
0
45273
Swiss-Prot
other Location (Reliability: 2)
PUS6_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
404
0
46816
Swiss-Prot
-
PUS7_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
676
0
77002
Swiss-Prot
-
PUS1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
544
0
62143
Swiss-Prot
-
PUS10_METJA
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
454
0
52927
Swiss-Prot
-
PUS10_PYRFU
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
388
0
44680
Swiss-Prot
-
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the hPus1p enzyme binds to its RNA substrate as a monomer. The C-terminal end of hPus1p folds into two alpha-helices and these helices pack against the back of the hPus1p molecule, which prevents the dimerization observed in the bacterial homologue, TruA. This C-terminal region is responsible for the atypical RNA substrate binding and activity of hPus1p. Enzyme crystal structure analysis, overview
additional information
-
the hPus1p enzyme binds to its RNA substrate as a monomer. The C-terminal end of hPus1p folds into two alpha-helices and these helices pack against the back of the hPus1p molecule, which prevents the dimerization observed in the bacterial homologue, TruA. This C-terminal region is responsible for the atypical RNA substrate binding and activity of hPus1p. Enzyme crystal structure analysis, overview
additional information
study of the oligomerisation in solution of purified recombinant yeast tRNA:pseudouridine synthetase Pus1 in the presence or absence oftRNA. The presence of the neutral detergent dodecyl-beta-D-maltoside helps in avoiding the oligomerization/inactivation of the purified Pus1 in the absence of tRNA
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant detagged truncated enzyme mutant . DELTAhPus1p and mutant D146A DELTAhPus1p, sitting drop technique, mixing of 7 mg/ml protein in 20 mM HEPES, pH 7.0, 150 mM NaCl, 5 mM MgCl2, and 5 mM TCEP, with an equal amount of reservoir solution containing for DELTAhPus1p crystals 28% PEG 3350/glycerol, 0.1 M Bicine/Tris, pH 8.5, 10% amino acids mixture (with 0.02 M sodium L-glutamate, 0.02 M DL-alanine, 0.02 M glycine, 0.02 M DL-lysine HCl, 0.02 M DL-serine), and for D146A DELTAhPus1p crystals 17% PEG 8000, and 0.1 M HEPES, pH 8.0, both at 4°C, for 2-3 days, X-ray diffraction structure determination and analysis at 2.0-2.7 A resolution, respectively, molecular replacement using Pus1p structure, PDB ID 4ITS, as a model
sitting drop technique. The crystal structure of the catalytic domain of hPus1p and the D146A mutant of the enzyme is determined at 2.0 A resolution, alone and in a complex with several molecules present during crystallisation
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
Y173F
Y173G
mutant enzyme retains some activity with yeast pre-tRNAIle. The activity is relatively low
Y173T
additional information
Y173F
mutant enzyme retains some activity with yeast pre-tRNAIle. The activity is relatively low
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 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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, tag cleavage by TEV protease, followed by gel filtration, to hoomogeneity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Saccharomyces cerevisiae
gene PUS1, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
recombinant Pus1, tagged with six histidine residues at its N-terminus is expressed in Escherichia coli
the PUS1 ORF is tagged at its amino-terminal end with six histidines and overexpressed in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
functional disruption of a chloroplast pseudouridine synthase desensitizes Arabidopsis plants to phosphate starvation
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Motorin, Y.; Keith, G.; Simon, C; Foiret, D.; Simos, G.; Hurt, E.; Grosjean, H.
The yeast tRNA: pseudouridine synthase Pus1p displays a multisite substrate specificity
RNA
4
856-869
1998
Saccharomyces cerevisiae (Q12211), Saccharomyces cerevisiae
brenda
Arluison, V.; Hountondji, C.; Robert, B.; Grosjean, H.
Transfer RNA-Pseudouridine Synthetase Pus1 of Saccharomyces cerevisiae contains one atom of zinc essential for its native conformation and tRNA recognition
Biochemistry
37
7268-7276
1998
Saccharomyces cerevisiae (Q12211)
brenda
Chen, J.; Patton, J.R.
Cloning and characterization of a mammalian pseudouridine synthase
RNA
5
409-419
1999
Mus musculus (Q9WU56), Mus musculus
brenda
Arluison, V.; Buckle, M.; Grosjean, H.
Pseudouridine synthetase Pus1 of Saccharomyces cerevisiae: kinetic characterisation, tRNA structural requirement and real-time analysis of its complex with tRNA
J. Mol. Biol.
289
491-502
1999
Saccharomyces cerevisiae (Q12211)
brenda
Arluison, V.; Batelier, G.; Ris-Kautt, M.; Grosjean, H.
RNA: pseudouridine synthase pus1 from Saccharomyces cerevisiae: oligomerization property and stoichiometry of the complex with yeast tRNA Phe
Biochimie
81
751-756
1999
Saccharomyces cerevisiae (Q12211)
brenda
Bykhovskaya, Y.; Casas, K.; Mengesha, E.; Inbal, A.; Fischel-Ghodsian, N.
Missense mutation in pseudouridine synthase 1 (PUS1) causes mitochondrial myopathy and sideroblastic anemia (MLASA)
Am. J. Hum. Genet.
74
1303-1308
2004
Homo sapiens (Q9Y606), Homo sapiens
brenda
Behm-Ansmant, I.; Massenet, S.; Immel, F.; Patton, J.R.; Motorin, Y.; Branlant, C.
A previously unidentified activity of yeast and mouse RNA:pseudouridine synthases 1 (Pus1p) on tRNAs
RNA
12
1583-1593
2006
Saccharomyces cerevisiae (Q12211), Saccharomyces cerevisiae, Mus musculus
brenda
Sibert, B.S.; Fischel-Ghodsian, N.; Patton, J.R.
Partial activity is seen with many substitutions of highly conserved active site residues in human Pseudouridine synthase 1
RNA
14
1895-1906
2008
Homo sapiens (Q9Y606), Homo sapiens
brenda
Simos, G.; Tekotte, H.; Grosjean, H.; Segref, A.; Sharma, K.; Tollervey, D.; Hurt, E.C.
Nuclear pore proteins are involved in the biogenesis of functional tRNA
EMBO J.
15
2270-2284
1996
Saccharomyces cerevisiae (Q12211)
brenda
Hellmuth, K.; Grosjean, H.; Motorin, Y.; Deinert, K.; Hurt, E.; Simos, G.
Cloning and characterization of the Schizosaccharomyces pombe tRNA:pseudouridine synthase Pus1p
Nucleic Acids Res.
28
4604-4610
2000
Schizosaccharomyces pombe (O94396), Schizosaccharomyces pombe
brenda
Schwartz, S.; Bernstein, D.A.; Mumbach, M.R.; Jovanovic, M.; Herbst, R.H.; Leon-Ricardo, B.X.; Engreitz, J.M.; Guttman, M.; Satija, R.; Lander, E.S.; Fink, G.; Regev, A.
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
J. Biol. Chem.
292
4519-4532
2017
Homo sapiens (Q96CM3)
brenda
Tillault, A.S.; Schultz, S.K.; Wieden, H.J.; Kothe, U.
Molecular determinants for 23S rRNA recognition and modification by the E. coli pseudouridine synthase RluE
J. Mol. Biol.
430
1284-1294
2018
Escherichia coli (P75966), Escherichia coli K12 (P75966)
brenda
Fitzek, E.; Joardar, A.; Gupta, R.; Geisler, M.
Evolution of eukaryal and archaeal pseudouridine synthase Pus10
J. Mol. Evol.
86
77-89
2018
Homo sapiens (Q3MIT2), Arabidopsis thaliana (F4HSS8), Methanocaldococcus jannaschii (Q60346), Pyrococcus furiosus (Q8U1R6)
brenda
Lovejoy, A.F.; Riordan, D.P.; Brown, P.O.
Transcriptome-wide mapping of pseudouridines pseudouridine synthases modify specific mRNAs in S. cerevisiae
PLoS ONE
9
e110799
2014
Saccharomyces cerevisiae (P48567), Saccharomyces cerevisiae (P53294), Saccharomyces cerevisiae (Q12211), Saccharomyces cerevisiae ATCC 204508 (Q12211), Saccharomyces cerevisiae ATCC 204508 (P48567), Saccharomyces cerevisiae ATCC 204508 (P53294)
brenda
Huet, T.; Miannay, F.A.; Patton, J.R.; Thore, S.
Steroid receptor RNA activator (SRA) modification by the human pseudouridine synthase 1 (hPus1p) RNA binding, activity, and atomic model
PLoS ONE
9
e94610
2014
Homo sapiens (Q9Y606), Homo sapiens
brenda
Deryusheva, S.; Gall, J.G.
Dual nature of pseudouridylation in U2 snRNA Pus1p-dependent and Pus1p-independent activities in yeasts and higher eukaryotes
RNA
23
1060-1067
2017
Schizosaccharomyces pombe, Caenorhabditis elegans, Drosophila melanogaster, Xenopus tropicalis, Saccharomyces cerevisiae, Mus musculus, Saccharomyces cerevisiae BY4741, Schizosaccharomyces pombe 972, Drosophila melanogaster yw
brenda
Nakamoto, M.A.; Lovejoy, A.F.; Cygan, A.M.; Boothroyd, J.C.
mRNA pseudouridylation affects RNA metabolism in the parasite Toxoplasma gondii
RNA
23
1834-1849
2017
Toxoplasma gondii (B6V6I8), Toxoplasma gondii
brenda
EXTERNAL LINKS (specific for EC-Number 5.4.99.B22)
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