Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
tRNA uridine55
tRNA pseudouridine55
tRNA uridine55
tRNA pseudouridine552
substrate: Escherichia coli tRNAPhe
-
-
?
tRNATrp uridine55
tRNATrp pseudouridine55
-
tRNATrp containing or lacking 3'-CCA. aCbf5 and aGar1 together can function as a tRNA Psi55 synthase in a guide RNA-independent manner. This activity is enhanced by aNop10, but not by L7Ae. The aCbf5 alone can also produce Psi55 in tRNAs that contain the canonical 3'-CCA sequence and this activity is stimulated by aGar1. tRNAs lacking 3'-CCA can be modified only by the aCbf5-aGar1 complex. The presence of conserved C (or U) and A at tRNA positions 56 and 58, respectively, is not essential for aCbf5-mediated Psi55 formation
-
-
?
additional information
?
-
tRNA uridine55
tRNA pseudouridine55
-
-
-
-
?
tRNA uridine55
tRNA pseudouridine55
-
-
-
?
tRNA uridine55
tRNA pseudouridine55
-
activity is determined with yeast tRNAPhe (wild-type and mutants). A 17 base oligoribonucleotide analog of the T-arm is equivalent to intact native tRNA as a substrate for pseudouridine 55 synthase. The structures and activities of mutant tRNAs and T-arms are used to analyze substrate recognition by pseudouridine 55 synthase. The 17-mer T-arm is an excellent substrate for the synthase, while disruption of the stem structure of the 17-mer T-arm eliminates activity. Kinetic data on tRNA mutants lacking single T-stem base pairs indicate that only the 53:61 base pair, which maintains the 7 base loop size, is essential for activity. The identities of individual bases in the stem are unimportant provided base pairing is intact. A major function of the T-stem appears to be the maintainence of a stable stem-loop structure and proper presentation of the T-loop to pseudouridine 55 synthase. The 7 base T-loop can be expanded or contracted by 1 base and still retains activity, albeit with a 30fold reduction in kcat. Kinetic analysis of T-loop mutants reveals the requirement for uridine54, uridine55, and adenine58, and a preference for cytosine over uridine at position 56
-
-
?
tRNA uridine55
tRNA pseudouridine55
substrate: Escherichia coli tRNAPhe
-
-
?
tRNA uridine55
tRNA pseudouridine55
the recombinant protein is specific for uridine55 in tRNA transcripts and reacts neither at other sites for PSI in such transcripts nor with transcripts of 16S or 23S ribosomal RNA or subfragments. Uridine54, uridine32 and uridine39 are not converted to pseudouridine. Stoichiometric formation of psi occurs with no requirement for an external source of energy, indicating that PSI synthesis is thermodynamically favored
-
-
?
tRNA uridine55
tRNA pseudouridine55
-
-
-
?
tRNA uridine55
tRNA pseudouridine55
-
-
-
-
?
tRNA uridine55
tRNA pseudouridine55
-
-
-
?
tRNA uridine55
tRNA pseudouridine55
-
aCbf5 and aGar1 together can function as a tRNA pseudouridine55 synthase in a guide RNA-independent manner. This activity is enhanced by aNop10, but not by L7Ae. The aCbf5 alone can also produce pseudouridine55 in tRNAs that contain the canonical 3-CCA sequence and this activity is stimulated by aGar1. The presence of C (or U) and A at tRNA position 56 and 58, respectively are not essential for Cbf5-mediated PSI55 formation. Variation in the structure of the anticodon arm of the tRNA does not affect the PSI55 synthase activity
-
-
?
tRNA uridine55
tRNA pseudouridine55
-
the bifunctional enzyme can act as synthase for both tRNA pseudouridine54 and pseudouridine55. The two modifications seem to occur independently. Unlike bacterial TruB and yeast Pus4, archaeal Pus10 does not require a U54*A58 reverse Hoogstein base pair and pyrimidine at position 56 to convert tRNA uridine55 to pseudouridine55. Although the T(PSI)PSI-arm of tRNA is a good substrate for both pseudouridine54 and pseudouridine55 synthesis by Mj-Pus10, the production of pseudouridine55 is more efficient than that of pseudouridine54 in this substrate. This contrasts with full-size tRNA substrates, where syntheses of pseudourines appear to be equally efficient
-
-
?
tRNA uridine55
tRNA pseudouridine55
the enzyme also exhibits tRNA pseudouridine54 synthase activity. The forefinger loop (reminiscent of that of RluA) and an Arg and a Tyr residue of archaeal Pus10 as critical determinants for its tRNA pseudouridine54 synthase, but not for its tRNA pseudouridine55 activity. A Leu residue, in addition to the catalytic Asp, is essential for both activities. Archaeal Pus10 proteins must use a different mechanism of recognition for tRNA pseudouridine55 than for the recognition of pseudouridine54. It is proposed that archaeal Pus10 uses two distinct mechanisms for substrate uridine recognition and binding. No mutation mutation is detected that affects only tRNA pseudouridine54 synthase activity, both mechanisms for archaeal Pus10 activities must share some common features
-
-
?
tRNA uridine55
tRNA pseudouridine55
the enzyme also exhibits tRNA pseudouridine54 synthase activity. The forefinger loop (reminiscent of that of RluA) and an Arg and a Tyr residue of archaeal Pus10 as critical determinants for its tRNA pseudouridine54 synthase, but not for its tRNA pseudouridine55 activity. A Leu residue, in addition to the catalytic Asp, is essential for both activities. Archaeal Pus10 proteins must use a different mechanism of recognition for tRNA pseudouridine55 than for the recognition of pseudouridine54. It is proposed that archaeal Pus10 uses two distinct mechanisms for substrate uridine recognition and binding. No mutation mutation is detected that affects only tRNA pseudouridine54 synthase activity, both mechanisms for archaeal Pus10 activities must share some common features
-
-
?
tRNA uridine55
tRNA pseudouridine55
the stable anchoring of aCBF5 to tRNAs relies on its PUA domain and the tRNA CCA sequence
-
-
?
tRNA uridine55
tRNA pseudouridine55
-
assay with T7-transcribed pfutRNAAsp. Two distinct pseudouridine synthases specifically modify uridine55 in tRNA in vitro: 1. Cbf5, a protein known to play a role in RNA-guided modification of rRNA, and 2. pfuPus10 is not a member of the TruB/Pus4/Cbf5 family of pseudouridine synthases. Pus10 can pseudouridylate a truncated tRNA substrate and a tRNA lacking the 3'CCA. Cbf5 functions only on the full-length tRNA substrate including the 3'CCA end
-
-
?
tRNA uridine55
tRNA pseudouridine55
-
uridine55 in Haloferax volcanii tRNATrp. The bifunctional enzyme can act as synthase for both tRNA pseudouridine54 and pseudouridine55. The two modifications seem to occur independently. Unlike bacterial TruB and yeast Pus4, archaeal Pus10 does not require a U54*A58 reverse Hoogstein base pair and pyrimidine at position 56 to convert tRNA U55 to C55
-
-
?
tRNA uridine55
tRNA pseudouridine55
Pus4 catalyses the formation of pseudouridine55 in both mitochondrial and cytoplasmic tRNAs
-
-
?
tRNA uridine55
tRNA pseudouridine55
the purified Pus4p catalyzes the formation of pseudouridine55 in T7 in vitro transcripts of several yeast tRNA genes. In contrast to the known yeast pseudouridine synthase (Pus1) of broad specificity, no other uridines in tRNA molecules are modified by the cloned recombinant Pus4p
-
-
?
tRNA uridine55
tRNA pseudouridine55
-
-
-
?
additional information
?
-
RNA containing 5-fluorouridine is a substrate
-
-
?
additional information
?
-
-
RNA containing 5-fluorouridine is a substrate
-
-
?
additional information
?
-
-
the enzyme binds much more weakly to small RNA Pab91 than to small RNA Pab21. The Pab91 small ribonucleoprotein particle exhibits a higher catalytic efficiency than the Pab21 small ribonucleoprotein particle. Efficient aCBF5 binding probably relies on the pseudouridylation pocket which is not optimized for high activity in the case of Pab21
-
-
?
additional information
?
-
efficient formation of 5-fluoro-6-hydroxypseudouridine55 from 5-fluorouridine55 is catalyzed by wild-type enzyme and mutant enzymes Y67F and Y67L
-
-
?
additional information
?
-
-
efficient formation of 5-fluoro-6-hydroxypseudouridine55 from 5-fluorouridine55 is catalyzed by wild-type enzyme and mutant enzymes Y67F and Y67L
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.011 - 0.78
tRNA uridine55
-
additional information
additional information
-
turnover numbers are determined for wild-type and mutant forms of yeast tRNAPhe. The 7 base T-loop can be expanded or contracted by 1 base and still retains activity, albeit with a 30fold reduction in kcat
-
0.011
tRNA uridine55
pH 7.5, 37°C, Escherichia coli tRNAPhe, mutant enzyme K19R
-
0.012
tRNA uridine55
pH 7.5, 37°C, Escherichia coli tRNAPhe, mutant enzyme K19M
-
0.11
tRNA uridine55
pH 7.5, 37°C, Escherichia coli tRNAPhe, wild-type enzyme
-
0.11
tRNA uridine55
pH 7.5, 37°C, substrate: Escherichia coli tRNAPhe, mutant enzyme C58A/C174A/C193A
-
0.12
tRNA uridine55
pH 7.5, 37°C, substrate: Escherichia coli tRNAPhe. wild-type enzyme
-
0.16
tRNA uridine55
pH 7.5, 37°C, substrate: Escherichia coli tRNAPhe, mutant enzyme C174A
-
0.18
tRNA uridine55
wild-type enzyme
-
0.18
tRNA uridine55
pH 7.5, 37°C, substrate: Escherichia coli tRNAPhe, mutant enzyme C193V
-
0.23
tRNA uridine55
pH 7.5, 37°C, Escherichia coli tRNAPhe, mutant enzyme P20G
-
0.24
tRNA uridine55
-
in yeast tRNAPhe, pH 8.0, 37°C
-
0.26
tRNA uridine55
pH 7.5, 37°C, substrate: Escherichia coli tRNAPhe, mutant enzyme C58A
-
0.52
tRNA uridine55
pH 7.5, 37°C, Escherichia coli tRNAPhe, mutant enzyme P20L
-
0.78
tRNA uridine55
pseudouridine synthase TruB with an 10-amino acid N-terminal truncation
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
-
the finding that in archaea Cbf5 may function in tRNA uridine55 pseudouridylation as well as RNA-guided pseudouridylation of rRNA supports the idea that Cbf5 is a direct descendant of a primordial TruB/Pus4-like tRNA PSI synthase
evolution
in archaea, pseudouridine (Psi) synthase Pus10 modifies uridine (U) to Psi at positions 54 and 55 of tRNA. Pus10 is not found in bacteria, where modifications at those two positions are carried out by TrmA (U54 to m5U54) and TruB (U55 to Psi55). Many eukaryotes have an apparent redundancy, their genomes contain orthologues of archaeal Pus10 and bacterial TrmA and TruB. 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). Examination of 116 archaeal and eukaryotic Pus10 protein sequences reveals that Pus10 exists as a single copy gene in all the surveyed genomes despite ancestral whole genome duplications had occurred. Functional redundancy result in gene loss or neofunctionalization in different evolutionary lineages. The enzyme is a member of the pseudouridine synthase superfamily with a similar three-dimensional structure and a conserved catalytic Asp. In the catalytic region, five amino acids (Asp275, Tyr339, Ile412, Lys413, Leu440 in Methanocalcoccus jannaschii) are conserved throughout all pseudouridine synthase families
evolution
in archaea, pseudouridine (Psi) synthase Pus10 modifies uridine (U) to Psi at positions 54 and 55 of tRNA. Pus10 is not found in bacteria, where modifications at those two positions are carried out by TrmA (U54 to m5U54) and TruB (U55 to Psi55). Many eukaryotes have an apparent redundancy, their genomes contain orthologues of archaeal Pus10 and bacterial TrmA and TruB. 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). Examination of 116 archaeal and eukaryotic Pus10 protein sequences reveals that Pus10 exists as a single copy gene in all the surveyed genomes despite ancestral whole genome duplications had occurred. Functional redundancy result in gene loss or neofunctionalization in different evolutionary lineages. The enzyme is a member of the pseudouridine synthase superfamily with a similar three-dimensional structure and a conserved catalytic Asp. In the catalytic region, five amino acids (Asp275, Tyr339, Ile412, Lys413, Leu440 in Methanocalcoccus jannaschii) are conserved throughout all pseudouridine synthase families
malfunction
-
a parallel lack of 2'-O-methylguanosine18 and pseudouridine55 in tRNA of Escherichia coli affects growth rate, translation of certain codons, sensitivity to amino acid analogs, and oxidation of some carbon compounds
malfunction
-
a truB mutation reduces the expression of some virulence-associated genes
malfunction
a truB null mutant grows normally on all growth media tested, but exhibits a competitive disadvantage in extended co-culture with its wild-type progenitor. The mutant phenotype can be complemented by both the cloned truB gene and by a D48C, catalytically inactive allele of truB. The truB mutant also exhibits a defect in survival of rapid transfer from 37 to 50°C
malfunction
deletion of the Escherichia coli pseudouridine synthase gene truB blocks formation of pseudouridine 55 in tRNA in vivo, does not affect exponential growth, but confers a strong selective disadvantage in competition with wild-type cells
malfunction
the disruption of the YNL292w gene in yeast, which has no significant effect on the growth of yeast cells, leads to the complete disappearance of the pseudouridine55 formation activity in a cell-free extract
physiological function
pseudouridine-55 synthase is responsible for modifying all tRNA molecules in the cell at the uridine55 position. TruB-effected pseudouridine55 modification of tRNA is not essential, but contributes to thermal stress tolerance in Escherichia. coli, possibly by optimizing the stability of the tRNA population at high temperatures
physiological function
human Pus10 participates in apoptosis induced by the tumor necrosis factor-related apoptosis-inducing ligand
additional information
homology modeling and structural superimposition using the crystal structure of Homo sapiens enzyme Pus10, PDB ID 2V9K, as a template, overview
additional information
the human enzyme crystal structure, PDB ID 2V9K, is modelled onto the structure of Methanocalcoccus jannaschii
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
C174A
kcat is 1.3fold higher than wild-type value, KM is 1.1fold lower than wild-type value
C193V
kcat is 1.5fold higher than wild-type value, KM is 1.5fold higher than wild-type value
C58A
kcat is 2.2fold higher than wild-type value, KM is 1.2fold higher than wild-type value
C58A/C174A/C193A
kcat is 1.1fold lower than wild-type value, KM is 1.2fold lower than wild-type value
D48N
inactive mutant enzyme
D90A
-
dissociation constant: 0.4 microM (wild-type: 0.7 microM), rate of pseudouridine formation compared to wild-type: 500fold decreased, rate of tRNA binding (kapp2): 2/sec (wild-type: 4.2/sec)
D90E
-
dissociation constant: 0.4 microM (wild-type: 0.7 microM), rate of pseudouridine formation compared to wild-type: 30fold decreased, rate of tRNA binding (kapp2): 1.5/sec (wild-type: 4.2/sec)
D90N
-
dissociation constant: 0.4 microM (wild-type: 0.7 microM), rate of pseudouridine formation compared to wild-type: 50fold decreased, rate of tRNA binding (kapp2): 1.9/sec (wild-type: 4.2/sec)
K19M
kcat is 8fold lower than wild-type value. KM-value is 11fold higher than wild-type value
K19R
kcat is 10fold lower than wild-type value. KM-value is 6fold higher than wild-type value
P20G
kcat is 4.8fold lower than wild-type value. KM-value is 2.2fold higher than wild-type value
P20L
kcat is 2.1fold lower than wild-type value. KM-value is 3.5fold higher than wild-type value
R181A
-
dissociation constant: 2 microM (wild-type: 0.7 microM), rate of pseudouridine formation compared to wild-type: more than 20000fold decreased, rate of tRNA binding (kapp2): 4/sec (wild-type: 4.2/sec)
R181K
-
dissociation constant: 0.7 microM (wild-type: 0.7 microM), rate of pseudouridine formation compared to wild-type: 2500fold decreased, rate of tRNA binding (kapp2): 1.9/sec (wild-type: 4.2/sec)
R181M
-
dissociation constant: 0.5 microM (wild-type: 0.7 microM), rate of pseudouridine formation compared to wild-type: more than 20000fold decreased, rate of tRNA binding (kapp2): 3/sec (wild-type: 4.2/sec)
C106A/C109A
decrease in tRNA pseudouridine54 synthase activity, no decrease in tRNA pseudouridine55 synthase activity
D275A
the mutant shows no tRNA pseudouridine54 synthase activity and no tRNA pseudouridine55 synthase activity
D277A
decrease in tRNA pseudouridine54 synthase activity and low decrease in tRNA pseudouridine55 synthase activity
H376A/R377A
decrease in tRNA pseudouridine54 synthase activity and in tRNA pseudouridine55 synthase activity
I412A
decrease in tRNA pseudouridine54 synthase activity and in tRNA pseudouridine55 synthase activity
K413A
decrease in tRNA pseudouridine54 synthase activity and in tRNA pseudouridine55 synthase activity
L440A
the mutant shows no tRNA pseudouridine54 synthase activity and no tRNA pseudouridine55 synthase activity
R273A
decrease in tRNA pseudouridine54 synthase activity and in tRNA pseudouridine55 synthase activity
Y339A
the mutant shows no tRNA pseudouridine54 synthase activity and no tRNA pseudouridine55 synthase activity
D275A
-
the mutant shows no tRNA pseudouridine54 synthase activity and no tRNA pseudouridine55 synthase activity
-
D277A
-
decrease in tRNA pseudouridine54 synthase activity and low decrease in tRNA pseudouridine55 synthase activity
-
I412A
-
decrease in tRNA pseudouridine54 synthase activity and in tRNA pseudouridine55 synthase activity
-
R273A
-
decrease in tRNA pseudouridine54 synthase activity and in tRNA pseudouridine55 synthase activity
-
Y339A
-
the mutant shows no tRNA pseudouridine54 synthase activity and no tRNA pseudouridine55 synthase activity
-
K53A
substitution K53A or R202A in aCBF5 impairs both the tRNA:pseudouridine55-synthase and the RNA-guided RNA:pseudouridine-synthase activities
R202A
substitution K53A or R202A in aCBF5 impairs both the tRNA:pseudouridine55-synthase and the RNA-guided RNA:pseudouridine-synthase activities
Y67F
no activity with the natural RNA substrate, efficient formation of 5-fluoro-6-hydroxypseudouridine55 from 5-fluorouridine55
Y67L
no activity with the natural RNA substrate, efficient formation of 5-fluoro-6-hydroxypseudouridine55 from 5-fluorouridine55
additional information
mutant enzymes with substitution of the nearly invariant lysine and proline residues in motif I of RluA display only very mild kinetic impairment. Substitution of the aligned lysine and proline residues reduces structural stability
additional information
substitution of cysteine for amino acids with nonnucleophilic side chains does not significantly alter the catalytic activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Becker, H.F.; Motorin, Y.; Planta, R.J.; Grosjean, H.
The yeast gene YNL292w encodes a pseudouridine synthase (Pus4) catalyzing the formation of psi 55 in both mitochondrial and cytoplasmatic tRNAs
Nucleic Acids Res.
25
4493-4499
1997
Saccharomyces cerevisiae (P48567), Saccharomyces cerevisiae
brenda
Ramamurthy, V.; Swann, S.; Spedaliere, C.; Mueller, E.
Role of cysteine residues in pseudouridine synhases of different families
Biochemistry
38
13106-13111
1999
Escherichia coli (P60340)
brenda
Hoang, C.; Ferre-D'Amare, A.R.
Cocrystal structure of a tRNA psi55 pseudouridine synthase: nucleotide flipping by an RNA-modifying enzyme
Cell
107
929-939
2001
Escherichia coli (P60340)
brenda
Chaudhuri, B.N.; Chan, S.; Perry, L.J.; Yeates, T.O.
Crystal structure of the apo forms of psi55 tRNA pseudouridine synthase from Mycobacterium tuberculosis. A hinge at the base of the catalytic cleft
J. Biol. Chem.
279
24585-24591
2004
Mycobacterium tuberculosis (P9WHP7), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WHP7)
brenda
Pan, H.; Agarwalla, S.; Moustakas, D.T.; Finer-Moore, J.; Stroud, R.M.
Structure of tRNA pseudouridine synthase TruB and its RNA complex: RNA recognition through a combination of rigid docking and induced fit
Proc. Natl. Acad. Sci. USA
100
12648-12653
2003
Escherichia coli (P60340), Thermotoga maritima (Q9WZW0)
brenda
Phannachet, K.; Elias, Y.; Huang, R.H.
Dissecting the roles of a strictly conserved tyrosine in substrate recognition and catalysis by pseudouridine 55 synthase
Biochemistry
44
15488-15494
2005
Thermotoga maritima (Q9WZW0), Thermotoga maritima
brenda
Hoang, C.; Hamilton, C.S.; Mueller, E.G.; Ferre-D'Amare, A.R.
Precursor complex structure of pseudouridine synthase TruB suggests coupling of active site perturbations to an RNA-sequestering peripheral protein domain
Protein Sci.
14
2201-2206
2005
Escherichia coli (P60340)
brenda
Gurha, P.; Gupta, R.
Archaeal Pus10 proteins can produce both pseudouridine 54 and 55 in tRNA
RNA
14
2521-2527
2008
Methanocaldococcus jannaschii, Pyrococcus furiosus
brenda
Pienkowska, J.; Wrzesinski, J.; Szweykowska-Kulinska, Z.
A cell-free yellow lupin extract containing activities of pseudouridine 35 and 55 synthases
Acta Biochim. Pol.
45
745-754
1998
Lupinus luteus
brenda
Gu, X.; Yu, M.; Ivanetich, K.M.; Santi, D.V.
Molecular recognition of tRNA by tRNA pseudouridine 55 synthase
Biochemistry
37
339-343
1998
Escherichia coli
brenda
Spedaliere, C.J.; Hamilton, C.S.; Mueller, E.G.
Functional importance of motif I of pseudouridine synthases: mutagenesis of aligned lysine and proline residues
Biochemistry
39
9459-9465
2000
Escherichia coli (P60340)
brenda
Urbonavicius, J.; Durand, J.M.; Bjrk, G.R.
Three modifications in the D and T arms of tRNA influence translation in Escherichia coli and expression of virulence genes in Shigella flexneri
J. Bacteriol.
184
5348-5357
2002
Escherichia coli, Shigella flexneri
brenda
Kinghorn, S.M.; O'Byrne, C.P.; Booth, I.R.; Stansfield, I.
Physiological analysis of the role of truB in Escherichia coli: a role for tRNA modification in extreme temperature resistance
Microbiology
148
3511-3520
2002
Escherichia coli (P60340)
brenda
Roovers, M.; Hale, C.; Tricot, C.; Terns, M.P.; Terns, R.M.; Grosjean, H.; Droogmans, L.
Formation of the conserved pseudouridine at position 55 in archaeal tRNA
Nucleic Acids Res.
34
4293-4301
2006
Pyrococcus furiosus
brenda
Muller, S.; Fourmann, J.B.; Loegler, C.; Charpentier, B.; Branlant, C.
Identification of determinants in the protein partners aCBF5 and aNOP10 necessary for the tRNA:Psi55-synthase and RNA-guided RNA:PSI-synthase activities
Nucleic Acids Res.
35
5610-5624
2007
Pyrococcus abyssi (Q9V1A5)
brenda
Gurha, P.; Joardar, A.; Chaurasia, P.; Gupta, R.
Differential roles of archaeal box H/ACA proteins in guide RNA-dependent and independent pseudouridine formation
RNA Biol.
4
101-109
2007
Methanocaldococcus jannaschii
brenda
Spedaliere, C.J.; Mueller, E.G.
Not all pseudouridine synthases are potently inhibited by RNA containing 5-fluorouridine
RNA
10
192-199
2004
Escherichia coli (P60340), Escherichia coli
brenda
Nurse, K.; Wrzesinski, J.; Bakin, A.; Lane, B.G.; Ofengand, J.
Purification, cloning, and properties of the tRNA PSI 55 synthase from Escherichia coli
RNA
1
102-112
1995
Escherichia coli (P60340), Escherichia coli
brenda
Gutgsell, N.; Englund, N.; Niu, L.; Kaya, Y.; Lane, B.G.; Ofengand, J.
Deletion of the Escherichia coli pseudouridine synthase gene truB blocks formation of pseudouridine 55 in tRNA in vivo, does not affect exponential growth, but confers a strong selective disadvantage in competition with wild-type cells
RNA
6
1870-1881
2000
Escherichia coli (P60340)
brenda
Fourmann, J.B.; Tillault, A.S.; Blaud, M.; Leclerc, F.; Branlant, C.; Charpentier, B.
Comparative study of two box H/ACA ribonucleoprotein pseudouridine-synthases: relation between conformational dynamics of the guide RNA, enzyme assembly and activity
PLoS One
8
e70313
2013
Pyrococcus abyssi
brenda
Joardar, A.; Jana, S.; Fitzek, E.; Gurha, P.; Majumder, M.; Chatterjee K, Geisler M, Gupta R.
Role of forefinger and thumb loops in production of Psi54 and Psi55 in tRNAs by archaeal Pus10
RNA
19
1279-1294
2013
Methanocaldococcus jannaschii (Q60346), Methanocaldococcus jannaschii DSM 2661 (Q60346)
brenda
Yang, W.; Zhao, S.; Jin, L.; Guo, Z.; Zhang, S.; Zhang, H.; Wang, D.
Purification, crystallization and preliminary X-ray crystallographic study of the tRNA pseudouridine synthase TruB from Streptococcus pneumoniae
Acta Crystallogr. Sect. F
69
759-761
2013
Streptococcus pneumoniae (Q97QJ3), Streptococcus pneumoniae
brenda
Friedt, J.; Leavens, F.M.; Mercier, E.; Wieden, H.J.; Kothe, U.
An arginine-aspartate network in the active site of bacterial TruB is critical for catalyzing pseudouridine formation
Nucleic Acids Res.
42
3857-3870
2014
Escherichia coli
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), Methanocaldococcus jannaschii (Q60346)
brenda