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Information on EC 5.4.99.B22 - multisite-specific tRNA pseudouridine synthase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q12211
for references in articles please use BRENDA:EC5.4.99.B22preliminary BRENDA-supplied EC number
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5.4.99.B22 multisite-specific tRNA pseudouridine synthaseSpecify your search results
Word Map
- 5.4.99.B22
-
pseudouridylation
- anemia
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sideroblastic
- myopathy
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dyskerin
-
anticodon
-
mlasa
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spliceosomal
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nuclear-encoded
- agriculture
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
hide(3 overall reactions are displayed. Show all (9)>>)
tRNA uridine65
=
tRNA pseudouridine65
tRNA uridine26
=
tRNA pseudouridine26
tRNA uridine27
=
tRNA pseudouridine27
Synonyms
pus1p, mpus1p, pseudouridine synthase 1, rpusd4, hpus1p, scpus1p, sppus1p, tgpus1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
multisite-specific tRNA-uridine uracil mutase
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
RPL11a mRNA uridine68
RPL11a mRNA pseudouridine68
the Pus1 enzyme is necessary and sufficient for pseudouridylation of RPL11a mRNA
-
-
?
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
-
-
?
KAR2 mRNA uridine
KAR2 mRNA pseudouridine
-
-
-
?
TEF1 mRNA uridine239
TEF1 mRNA pseudouridine239
-
-
-
?
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
-
-
?
additional information
?
-
Pus1p catalyzes the formation of pseudouridines in several positions and in a number of different tRNA species
-
-
?
additional information
?
-
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Pus1p catalyzes the formation of pseudouridines in several positions and in a number of different tRNA species
-
-
?
additional information
?
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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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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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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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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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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
RPL11a mRNA uridine68
RPL11a mRNA pseudouridine68
the Pus1 enzyme is necessary and sufficient for pseudouridylation of RPL11a mRNA
-
-
?
KAR2 mRNA uridine
KAR2 mRNA pseudouridine
-
-
-
?
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
-
-
?
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
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00074
tRNAIle uridine27
pH and temperature not specified in the publication
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0.00042
tRNAVal uridine27
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
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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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
the disruption of the Pus1 gene confers no obvious phenotype
metabolism
the Pus1 enzyme is necessary and sufficient for pseudouridylation of RPL11a mRNA
evolution
-
Pus1p is a member of the TruA pseudouridine synthase family
physiological function
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
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
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)
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)
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)
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
Mus musculus, Saccharomyces cerevisiae (Q12211), Saccharomyces cerevisiae
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)
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)
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 (P48567), Saccharomyces cerevisiae ATCC 204508 (P53294), Saccharomyces cerevisiae ATCC 204508 (Q12211)
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
Caenorhabditis elegans, Drosophila melanogaster, Drosophila melanogaster yw, Mus musculus, Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741, Schizosaccharomyces pombe, Schizosaccharomyces pombe 972, Xenopus tropicalis
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