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Information on EC 2.1.1.207 - tRNA (cytidine34-2'-O)-methyltransferase and Organism(s) Escherichia coli and UniProt Accession P0AGJ7
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2.1.1.207 tRNA (cytidine34-2'-O)-methyltransferaseIUBMB Comments
The enzyme from Escherichia coli catalyses the 2'-O-methylation of cytidine or 5-carboxymethylaminomethyluridine at the wobble position at nucleotide 34 in tRNALeuCmAA and tRNALeucmnm5UmAA. The enzyme is selective for the two tRNALeu isoacceptors and only methylates these when they present the correct anticodon loop sequence and modification pattern. Specifically, YibK requires a pyrimidine nucleoside at position 34, it has a clear preference for an adenosine at position 35, and it fails to methylate without prior addition of the N6-(isopentenyl)-2-methylthioadenosine modification at position 37.
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
+
cytidine34 in tRNA
=
+
2'-O-methylcytidine34 in tRNA
+
=
+
+
5-carboxymethylaminomethyluridine34 in tRNALeu
=
+
5-carboxymethylaminomethyl-2'-O-methyluridine34 in tRNALeu
Synonyms
trna (um34/cm34) methyltransferase, trna (cytidine/uridine-2'o)-ribose methyltransferase l, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
tRNA (cytidine34/5-carboxymethylaminomethyluridine34'-O)-methyltransferase
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNA (cytidine34/5-carboxymethylaminomethyluridine34-2'-O)-methyltransferase
The enzyme from Escherichia coli catalyses the 2'-O-methylation of cytidine or 5-carboxymethylaminomethyluridine at the wobble position at nucleotide 34 in tRNALeuCmAA and tRNALeucmnm5UmAA. The enzyme is selective for the two tRNALeu isoacceptors and only methylates these when they present the correct anticodon loop sequence and modification pattern. Specifically, YibK requires a pyrimidine nucleoside at position 34, it has a clear preference for an adenosine at position 35, and it fails to methylate without prior addition of the N6-(isopentenyl)-2-methylthioadenosine modification at position 37.
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
S-adenosyl-L-methionine + 5-carboxymethylaminomethyluridine34 in tRNALeu
S-adenosyl-L-homocysteine + 5-carboxymethylaminomethyl-2'-O-methyluridine34 in tRNALeu
S-adenosyl-L-methionine + cytidine34 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine34 in tRNA
S-adenosyl-L-methionine + cytidine34 in tRNALeuCAA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine34 in tRNALeuCAA
S-adenosyl-L-methionine + cytidine34 in tRNALeuUAA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine34 in tRNALeuUAA
-
-
-
?
S-adenosyl-L-methionine + 5-carboxymethylaminomethyluridine34 in tRNA
S-adenosyl-L-homocysteine + 5-carboxymethylaminomethyl-2'-O-methyluridine34 in tRNA
S-adenosyl-L-methionine + cytidine34 in tRNALeuCAA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine34 in tRNALeuCAA
-
-
-
-
?
S-adenosyl-L-methionine + cytidine34 in tRNALeuUAA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine34 in tRNALeuUAA
-
-
-
-
?
S-adenosyl-L-methionine + 5-carboxymethylaminomethyluridine34 in tRNALeu
S-adenosyl-L-homocysteine + 5-carboxymethylaminomethyl-2'-O-methyluridine34 in tRNALeu
-
-
-
?
S-adenosyl-L-methionine + 5-carboxymethylaminomethyluridine34 in tRNALeu
S-adenosyl-L-homocysteine + 5-carboxymethylaminomethyl-2'-O-methyluridine34 in tRNALeu
the enzyme methylates the ribose at the nucleotide 34 wobble position in the two leucyl isoacceptors tRNALeu(CmAA) and tRNALeu(cmnm5UmAA)
-
-
?
S-adenosyl-L-methionine + cytidine34 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine34 in tRNA
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-
-
?
S-adenosyl-L-methionine + cytidine34 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine34 in tRNA
the enzyme methylates the ribose at the nucleotide 34 wobble position in the two leucyl isoacceptors tRNALeu(CmAA) and tRNALeu(cmnm5UmAA)
-
-
?
S-adenosyl-L-methionine + cytidine34 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine34 in tRNA
the enzyme methylates the ribose at the nucleotide 34 wobble position in the two leucyl isoacceptors tRNALeu(CmAA) and tRNALeu(cmnm5UmAA). No methylation of fully synthetic in vitro transcrips of tRNA(CAA), lacking all natural modifications present in in vivo transcripts. The motifs in tRNALeu required for YibK recognition and catalysis include the N6-(isopentenyl)-2-methylthioadenosine (ms2i6A) at position 37 and a pyridine at position 34. It has a clear preference for adenosine at position 35
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-
?
S-adenosyl-L-methionine + cytidine34 in tRNALeuCAA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine34 in tRNALeuCAA
-
-
-
?
S-adenosyl-L-methionine + cytidine34 in tRNALeuCAA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine34 in tRNALeuCAA
diverse mutant variants of tRNALeuCAA, overview
-
-
?
S-adenosyl-L-methionine + 5-carboxymethylaminomethyluridine34 in tRNA
S-adenosyl-L-homocysteine + 5-carboxymethylaminomethyl-2'-O-methyluridine34 in tRNA
-
TrmL catalyzes the methyl transfer from SAM to the 2'-OH of the wobble nucleotide in tRNALeu cmnm5UmAA, which decodes codons UUA and UUG in the Phe/Leu mixed box, and tRNALeu CmAA, which reads the UUG codon included in the Leu family box
o.e. tRNALeucmnm5UmAA
-
?
S-adenosyl-L-methionine + 5-carboxymethylaminomethyluridine34 in tRNA
S-adenosyl-L-homocysteine + 5-carboxymethylaminomethyl-2'-O-methyluridine34 in tRNA
-
TrmL catalyzes the methyl transfer from SAM to the 2'-OH of the wobble nucleotide in tRNALeu cmnm5UmAA, which decodes codons UUA and UUG in the Phe/Leu mixed box, and tRNALeu CmAA, which reads the UUG codon included in the Leu family box. The wobble nucleoside in tRNALeu cmnm5UmAA and tRNALeuCmAA is not thiolated. Nevertheless methylation of the 2'-hydroxyl group favors the C3'-endo ribose conformation for all nucleosides, although the effect is more marked with pyrimidines
o.e. tRNALeucmnm5UmAA
-
?
additional information
?
-
anticodon stem-loop minihelices with an extension of 2 base pairs are the minimal substrate for EcTrmL methylation. A35 is a key residue for TrmL recognition, while A36-A37-A38 are important either via direct interaction with TrmL or due to the necessity for prior isopentenylation (i6) at A37. In addition, TrmL only methylates pyrimidines but not purine residues at the wobble position, and the 20-O-methylation relies on prior N6-isopentenyladenosine modification at position 37. tRNALeuCAA and tRNALeuUAA isoacceptors are the only two RNA substrates of TrmL. i6A37 is sufficient to restore 20-O-methylation at C34 of EctRNALeuCAA transcripts in vitro. TrmL activity is sensitive to the modified base at position 37, a defect in synthesis of ms2i6A37 at position 37, leads to the loss of 20-O-methylation at C/U 34 at tRNALeuCAA and tRNALeuUAA isoacceptors.16 The isopentenyl modification at position 37 of transcribed tRNALeu is sufficient to recruit TrmL for methylation of nucleotides C34/U34. Although the affinity of i6A-Ts-tRNALeu CAA to EcTrmL is lower than for wild-type EctRNALeuCAA, the i6A modification has a consequent effect on the binding strength of tRNA transcripts for EcTrmL
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-
?
additional information
?
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the C/U34m modification occurs in leucine tRNACmAA and tRNAcmnm5UmAA. Both of these leucine tRNA isoacceptors recognize UUA-Leu and UUG-Leu codons, and also carry the i6A37 tRNA modification that assists in the optimal decoding of the Leu codons during rpoS translation
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-
-
additional information
?
-
-
the C/U34m modification occurs in leucine tRNACmAA and tRNAcmnm5UmAA. Both of these leucine tRNA isoacceptors recognize UUA-Leu and UUG-Leu codons, and also carry the i6A37 tRNA modification that assists in the optimal decoding of the Leu codons during rpoS translation
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-
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additional information
?
-
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in addition to a pyrimidine at position 34, the enzyme requires the presence of N6-(isopentenyl)-2-methylthioadenosine (ms2i6A) at position 37 as a positive identity determinant. Modification i6A, produced by MiaA, is enough to promote recognition of the substrate tRNAs by TrmL. Recognition of an amber codon by the supP suppressor, which is a mutant tRNALeu CmAA carrying the A35U change in the anticodon, is impaired if the suppressor lacks the 2'-O-methylation at the wobble position
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-
?
additional information
?
-
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the enzyme TrmL can independently catalyze the methyl transfer from S-adenosyl-L-methionine to tRNALeuCAA and tRNALeuUAA isoacceptors without the involvement of other tRNA-binding proteins. EcTrmL alone can efficiently methylate both tRNALeuCAA and tRNALeuUAA isoacceptors by using in vivo-purified tRNA substrates with certain modifications, but not unmodified tRNALeu
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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
S-adenosyl-L-methionine + 5-carboxymethylaminomethyluridine34 in tRNALeu
S-adenosyl-L-homocysteine + 5-carboxymethylaminomethyl-2'-O-methyluridine34 in tRNALeu
S-adenosyl-L-methionine + cytidine34 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine34 in tRNA
S-adenosyl-L-methionine + cytidine34 in tRNALeuCAA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine34 in tRNALeuCAA
-
-
-
?
S-adenosyl-L-methionine + cytidine34 in tRNALeuUAA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine34 in tRNALeuUAA
-
-
-
?
S-adenosyl-L-methionine + 5-carboxymethylaminomethyluridine34 in tRNA
S-adenosyl-L-homocysteine + 5-carboxymethylaminomethyl-2'-O-methyluridine34 in tRNA
-
TrmL catalyzes the methyl transfer from SAM to the 2'-OH of the wobble nucleotide in tRNALeu cmnm5UmAA, which decodes codons UUA and UUG in the Phe/Leu mixed box, and tRNALeu CmAA, which reads the UUG codon included in the Leu family box
o.e. tRNALeucmnm5UmAA
-
?
S-adenosyl-L-methionine + 5-carboxymethylaminomethyluridine34 in tRNALeu
S-adenosyl-L-homocysteine + 5-carboxymethylaminomethyl-2'-O-methyluridine34 in tRNALeu
-
-
-
?
S-adenosyl-L-methionine + 5-carboxymethylaminomethyluridine34 in tRNALeu
S-adenosyl-L-homocysteine + 5-carboxymethylaminomethyl-2'-O-methyluridine34 in tRNALeu
the enzyme methylates the ribose at the nucleotide 34 wobble position in the two leucyl isoacceptors tRNALeu(CmAA) and tRNALeu(cmnm5UmAA)
-
-
?
S-adenosyl-L-methionine + cytidine34 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine34 in tRNA
-
-
-
?
S-adenosyl-L-methionine + cytidine34 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine34 in tRNA
the enzyme methylates the ribose at the nucleotide 34 wobble position in the two leucyl isoacceptors tRNALeu(CmAA) and tRNALeu(cmnm5UmAA)
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-adenosyl-L-methionine
-
analysis of the structure of the cofactor binding pocket
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00182 - 0.00537
cytidine34 in tRNALeuCAA
wild-type tRNALeuCAA and diverse mutants thereof, pH 7.5, 37°C
-
additional information
additional information
-
steady-state kinetic parameters of EcTrmL with modified tRNALeu substrates
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0073 - 0.2
cytidine34 in tRNALeuCAA
wild-type tRNALeuCAA and diverse mutants thereof, pH 7.5, 37°C
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
role of several tRNA modifications on rpoS or hfq expression: 2'-O-methylation of cytidine or uridine, at the wobble position (C/Um), 2-thiouridine at the wobble position (s2U), as well as isopentenyl adenosine 37(i6A37), overview
physiological function
evolution
metabolism
-
modifications at the wobble uridine, U34, of tRNAs reading two degenerate codons ending in purine are complex and result from the activity of two multi-enzyme pathways, the IscSeMnmA and MnmEG pathways, which independently work on positions 2 and 5 of the U34 pyrimidine ring, respectively, and from a third single-step pathway, controlled by TrmL, i.e. YibK, that modifies the 2'-hydroxyl group of the ribose. TrmL occurs as a late step in the maturation of the tRNALeu isoacceptors
additional information
malfunction
inactivation of yibK leads to loss of 2'-O-methylation at position 34 in both tRNALeu(CmAA) and tRNALeu(cmnm5UmAA). Loss of YibK methylation reduces the efficiency of codonwobble base interaction. Inactivation of yibK has no detectable effect on steady-state growth rate, although a distinct disadvantage is noted in multiple-round, mixed-population growth experiments, suggesting that the ability to recover from the stationary phase is impaired. Methylation is restored in vivo by complementing with a recombinant copy of yibK
malfunction
the defect in RpoS translation in the absence of i6A37 prenyl transferase (MiaA) is due to the inability to add the C/U34m modification to UUX-Leu tRNAs
physiological function
TrmL is the prokaryotic methyltransferase that catalyzes the transfer of the methyl group from S-adenosyl-L-methionine to the wobble base of tRNALeuCAA and tRNALeuUAA isoacceptors. This Cm34/Um34 modification affects codon-anticodon interactions and is essential for translational fidelity
physiological function
the addition of the 2'-O-methylcytidine/uridine 34 (C/U34m) tRNA modification by tRNA (cytidine/uridine-2'O)-ribose methyltransferase L (TrmL) in Escherichia coli requires the presence of the N6-isopentenyl adenosine 37 (i6A37). The C/U34m and s2U34 tRNA modifications are necessary for full proper rpoS translation. Gene trmL is necessary for leucine decoding during RpoS expression. The mechanism of action of the i6A37 tRNA modification on RpoS expression is, at least in part, promotion of efficient UUX-leucine decoding. Possibly the TrmL-catalyzed C/U34m tRNA modification is dispensable for hfq translation, while the MiaA catalyzed i6A37 is necessary for efficient hfq translation
evolution
-
TrmL is a representative protein of SPOUTenzymes, a class of S-adenosyl-L-methionine-dependent methyltransferases that exhibit an unusual fold with a very deep topological knot. TrmL is one of the smallest alpha/beta-knot proteins
evolution
-
TrmL is a member of the SPOUT superfamily. TrmH, TrmJ and TrmL belong to the SpoU family, and TrmD belongs to the TrmD family. Unlike other transfer RNAs (tRNA)-modifying enzymes from the SPOUT methyltransferase superfamily, the tRNA (Um34/Cm34) methyltransferase TrmL lacks the usual extension domain for tRNA binding and consists only of a SPOUT domain. Domain architectures of SPOUT tRNA MTases and the sequence alignment of TrmLs, overview. TrmL enzymes are widely distributed throughout the bacterial kingdom
additional information
TrmL-catalyzed 2'-O-methylation requires its homodimerization. TrmL exhibits a fine-tuned tRNA substrate recognition mechanism. The variable arm of tRNA is not a recognition element for EcTrmL. The anticodon stem of tRNA does not contain recognition elements for EcTrmL
additional information
-
the enzyme TrmL functions as a homodimer by using the conserved C-terminal half of the SPOUT domain for catalysis, whereas residues from the less-conserved N-terminal half of the other subunit participate in tRNA recognition. Analysis of the structure of the active site. EcTrmL dimer formation is essential for tRNA recognition. The residue Y142 is critical for maintaining the dimeric form of EcTrmL, which is consistent with its central position at the interface
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
19800
-
2 * 19800, SDS-PAGE and gel filtration, the overall structure of an EcTrmL monomer subunit is composed of six beta-strands and six alpha-helices, in the order beta1-alpha1-beta2-alpha2-alpha3-beta3-alpha4-beta4-beta5-alpha5-beta6-alpha6. EcTrmL dimer formation is essential for tRNA recognition. The residue Y142 is critical for maintaining the dimeric form of EcTrmL, which is consistent with its central position at the interface
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
-
2 * 19800, SDS-PAGE and gel filtration, the overall structure of an EcTrmL monomer subunit is composed of six beta-strands and six alpha-helices, in the order beta1-alpha1-beta2-alpha2-alpha3-beta3-alpha4-beta4-beta5-alpha5-beta6-alpha6. EcTrmL dimer formation is essential for tRNA recognition. The residue Y142 is critical for maintaining the dimeric form of EcTrmL, which is consistent with its central position at the interface
additional information
TrmL-catalyzed 2'-O-methylation requires its homodimerization
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme TrmL in apoform and in complex with S-adenosyl-homocysteine, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement using the structure of Haemophilus influenzae Yibk, PDB ID 1J85 as starting search model, modeling
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K81E
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R104E
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R28E
-
site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme
R64E
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R74E
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y142A
-
site-directed mutagenesis, the mutant is a monomer in contrast to the wild-type enzyme. Mutant Y142A fails to form a complex with tRNA
additional information
additional information
generation of trmL+ and trmL- PBAD-rpoS990-lacZ translational fusions (in rssB- backgrounds) cells, executed for PBAD-rpoS990-lacZ translational fusions with rpoS UUA-Leu CUX-Leu mutations (leu*1)-strains KMT36002 and KMT36010, for rpoS UUG-Leu to CUX-leu mutation (leu*2)-strains KMT37002 and KMT37010, and for rpoS with both UUA-Leu to CUX-Leu and UUG-Leu to CUX-Leu mutations (leu*3)-strains KMT33001 and KMT33013, overview. Comparison of expression of PBAD-rpoS990-lacZ translational fusions carrying wild-type UUX leucine codons with derivatives in which UUX codons are changed to CUX codons, in the presence and absence of TrmL or TusA. The absence of these proteins, and therefore presumably the modifications they catalyze, both abolish PBAD-rpoS990-lacZ translation activity. UUX-Leu to CUX-Leu codon mutations in rpoS suppress the trmL requirement for PBAD-rpoS990-lacZ expression
additional information
-
generation of trmL+ and trmL- PBAD-rpoS990-lacZ translational fusions (in rssB- backgrounds) cells, executed for PBAD-rpoS990-lacZ translational fusions with rpoS UUA-Leu CUX-Leu mutations (leu*1)-strains KMT36002 and KMT36010, for rpoS UUG-Leu to CUX-leu mutation (leu*2)-strains KMT37002 and KMT37010, and for rpoS with both UUA-Leu to CUX-Leu and UUG-Leu to CUX-Leu mutations (leu*3)-strains KMT33001 and KMT33013, overview. Comparison of expression of PBAD-rpoS990-lacZ translational fusions carrying wild-type UUX leucine codons with derivatives in which UUX codons are changed to CUX codons, in the presence and absence of TrmL or TusA. The absence of these proteins, and therefore presumably the modifications they catalyze, both abolish PBAD-rpoS990-lacZ translation activity. UUX-Leu to CUX-Leu codon mutations in rpoS suppress the trmL requirement for PBAD-rpoS990-lacZ expression
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene trmL, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Benitez-Paez, A.; Villarroya, M.; Douthwaite, S.; Gabaldon, T.; Armengod, M.E.
YibK is the 2'-O-methyltransferase TrmL that modifies the wobble nucleotide in Escherichia coli tRNA(Leu) isoacceptors
RNA
16
2131-2143
2010
Escherichia coli (P0AGJ7)
Armengod, M.E.; Moukadiri, I.; Prado, S.; Ruiz-Partida, R.; Benitez-Paez, A.; Villarroya, M.; Lomas, R.; Garzon, M.J.; Martinez-Zamora, A.; Meseguer, S.; Navarro-Gonzalez, C.
Enzymology of tRNA modification in the bacterial MnmEG pathway
Biochimie
94
1510-1520
2012
Escherichia coli
Liu, R.J.; Zhou, M.; Fang, Z.P.; Wang, M.; Zhou, X.L.; Wang, E.D.
The tRNA recognition mechanism of the minimalist SPOUT methyltransferase, TrmL
Nucleic Acids Res.
41
7828-7842
2013
Escherichia coli, Escherichia coli MT102
Zhou, M.; Long, T.; Fang, Z.P.; Zhou, X.L.; Liu, R.J.; Wang, E.D.
Identification of determinants for tRNA substrate recognition by Escherichia coli C/U34 2-O-methyltransferase
RNA Biol.
12
900-911
2015
Escherichia coli (P0AGJ7)
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