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Information on EC 2.1.1.34 - tRNA (guanosine18-2'-O)-methyltransferase and Organism(s) Thermus thermophilus and UniProt Accession Q5SM16
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2.1.1.34 tRNA (guanosine18-2'-O)-methyltransferaseIUBMB Comments
The enzyme catalyses the methylation of guanosine18 in tRNA.
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Word Map
- 2.1.1.34
- thermophilus
-
thermus
-
d-loops
- ribose
- methyltransferases
- trnaphe
- adomet
-
2'-o-methyltransferases
- 2'-o-methylguanosine
- analysis
- s-adenosyl-l-homocysteine
- medicine
-
methyl-transfer
The taxonomic range for the selected organisms is: Thermus thermophilus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
+
=
+
+
guanosine18 in tRNA
=
+
2'-O-methylguanosine18 in tRNA
Synonyms
tarbp1, trna (gm18) methyltransferase, transfer rna (gm18) methyltransferase, trna (gm18) 2'-o-methyltransferase, trna gm18 methyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
methyltransferase, transfer ribonucleate guanosine 2'-
-
-
-
-
S-adenosyl-L-methionine:tRNA (guanosine-2'-O-)-methyltransferase
-
-
-
-
transfer ribonucleate guanosine 2'-methyltransferase
-
-
-
-
TrmH
tRNA (guanosine-2'-O-)-methyltransferase
-
-
-
-
tRNA guanosine 2'-methyltransferase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + guanosine18 in tRNA = S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in tRNA
S-adenosyl-L-methionine + guanosine18 in tRNA = S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in tRNA
S-adenosyl-L-methionine + guanosine18 in tRNA = S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in tRNA
methylation site
Q9FAC4
S-adenosyl-L-methionine + guanosine18 in tRNA = S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in tRNA
mechanism, upon binding of guanine 18, a RNA main chain phosphate group activates R41, which then deprotonates the 2'-OH-group for methylation
Q9FAC4
S-adenosyl-L-methionine + guanosine18 in tRNA = S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in tRNA
substrate recognition sites and mechanism
-
S-adenosyl-L-methionine + guanosine18 in tRNA = S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in tRNA
G18, G19 and the D-stem of the tRNA are required for Gm-methylase recognition
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNA (guanosine18-2'-O)-methyltransferase
The enzyme catalyses the methylation of guanosine18 in tRNA.
CAS REGISTRY NUMBER
COMMENTARY
37257-01-5
-
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 + guanosine18 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in tRNA
Q9FAC4
methylation at 2'-OH specifically of unmodified G18 of the ribose in the D-loop of tRNA
-
?
S-adenosyl-L-methionine + guanosine18 in yeast tRNA-Phe
S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in yeast tRNA-Phe
Q9FAC4
-
-
-
?
S-adenosyl-L-methionine + guanosine18 in yeast tRNAPhe
S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in yeast tRNAPhe
Q9FAC4
-
-
-
?
S-adenosyl-L-methionine + tRNA
S-adenosyl-L-homocysteine + tRNA containing 2'-O-methylguanine
Q9FAC4
-
-
-
?
S-adenosyl-L-methionine + Escherichia coli tRNA-Met
S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in Escherichia coli tRNA-Met
-
-
-
-
?
S-adenosyl-L-methionine + guanosine18 in Escherichia coli tRNA-Ile
S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in Escherichia coli tRNA-Ile
-
-
-
-
?
S-adenosyl-L-methionine + guanosine18 in Escherichia coli tRNA-Phe
S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in Escherichia coli tRNA-Phe
-
-
-
-
?
S-adenosyl-L-methionine + guanosine18 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in tRNA
S-adenosyl-L-methionine + guanosine18 in tRNAPhe
S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in tRNAPhe
substrate yeast tRNAPhe
-
-
?
S-adenosyl-L-methionine + guanosine18 in tRNATyr
S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in tRNATyr
-
involved in post-transcriptional tRNA modification
-
-
?
S-adenosyl-L-methionine + guanosine18 in yeast tRNA-Phe
S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in yeast tRNA-Phe
-
-
-
-
?
S-adenosyl-L-methionine + guanosine18 in yeast tRNAPhe mutant transcript
S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in yeast tRNAPhe mutant transcript
-
-
-
-
?
S-adenosyl-L-methionine + guanosine18 in yeast tRNAPhe-AGA mutant transcript
S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in yeast tRNAPhe-AGA mutant transcript
-
-
-
-
?
S-adenosyl-L-methionine + guanosine18 in yeast tRNAPhe-dG18 mutant transcript
S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in yeast tRNAPhe-dG18 mutant transcript
-
-
-
-
?
S-adenosyl-L-methionine + guanosine18 in yeast tRNAPhe-GAA mutant transcript
S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in yeast tRNAPhe-GAA mutant transcript
-
-
-
-
?
S-adenosyl-L-methionine + guanosine18 in yeast tRNAPhe-GGA mutant transcript
S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in yeast tRNAPhe-GGA mutant transcript
-
-
-
-
?
S-adenosyl-L-methionine + guanosine18 in yeast tRNAPhe-GUA mutant transcript
S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in yeast tRNAPhe-GUA mutant transcript
-
-
-
-
?
S-adenosyl-L-methionine + tRNA
S-adenosyl-L-homocysteine + tRNA containing 2'-O-methylguanine
-
-
-
-
?
S-adenosyl-L-methionine + yeast tRNA-Phe
S-adenosyl-L-homocysteine + yeast tRNA-Phe containing 2'-O-methylguanine
-
-
-
-
?
S-adenosyl-L-methionine + guanosine18 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in tRNA
-
methylation at 2'-OH specifically of unmodified G18 of the ribose in the D-loop of tRNA
-
?
S-adenosyl-L-methionine + guanosine18 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in tRNA
-
methylation at 2'-OH specifically of unmodified G18 of the ribose in the D-loop of tRNA
-
-
?
S-adenosyl-L-methionine + guanosine18 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in tRNA
-
methylation at 2'-OH specifically of unmodified G18 of the ribose in the D-loop of tRNA
-
?
S-adenosyl-L-methionine + guanosine18 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in tRNA
-
methyl group acceptor from yeast: tRNAPhe
-
?
S-adenosyl-L-methionine + guanosine18 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in tRNA
-
methyl group acceptor from yeast: tRNAPhe
-
-
?
S-adenosyl-L-methionine + guanosine18 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in tRNA
-
methyl group acceptor from yeast: tRNAPhe
-
?
S-adenosyl-L-methionine + guanosine18 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in tRNA
-
methyl group acceptor from yeast: tRNAPhe
-
?
S-adenosyl-L-methionine + guanosine18 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in tRNA
-
methyl group acceptors from E. coli: methyl deficient tRNATyr, tRNAPhe, tRNAfMet
-
?
S-adenosyl-L-methionine + guanosine18 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in tRNA
-
methyl group acceptors from E. coli: methyl deficient tRNATyr, tRNAPhe, tRNAfMet
-
-
?
S-adenosyl-L-methionine + guanosine18 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in tRNA
-
methyl group acceptors from Bacillus subtilis: tRNAVal, tRNALys, tRNAThr, tRNALeu
-
-
?
S-adenosyl-L-methionine + guanosine18 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in tRNA
-
substrate tRNAs from E. coli, yeast, Bacillus subtilis
-
?
additional information
?
-
-
specifically methylates guanosine at position 18 in the D-loop of tRNAPhe from E. coli
-
-
?
additional information
?
-
-
specifically methylates guanosine at position 18 in the D-loop of tRNAPhe from E. coli
-
-
?
additional information
?
-
-
specifically methylates guanosine at position 18 in the D-loop of tRNAPhe from E. coli
-
-
?
additional information
?
-
-
specifically methylates guanosine at position 18 in the D-loop of tRNAPhe from E. coli
-
-
?
additional information
?
-
-
specifically methylates guanosine at position 18 in the D-loop of tRNAPhe from E. coli
-
-
?
additional information
?
-
-
enzyme hydroxylates guanosine at postion 18 in tRNA
-
-
?
additional information
?
-
-
yeast tRNAPhe mutant transcripts are prepared in which the modification site and/or other nucleotides in the D-loop are substituted by dG, inosine, or other nucleotides. Sites of methylation are confirmed with RNA sequencing or primer extension. Although the G18G19 sequence is not essential for methylation by TrmH, disruption of G18G19 severely reduces the efficiency of methyl transfer. There is strict recognition of guanosine by TrmH, in that methylation occurs at the adjacent G19 when the G18 is replaced by dG or adenosine. The fact that TrmH methylates guanosine in D-loops from 4 to 12 nucleotides in length suggests that selection of the position of guanosine within the D-loop is relatively flexible
-
-
?
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 + guanosine18 in tRNATyr
S-adenosyl-L-homocysteine + 2'-O-methylguanosine18 in tRNATyr
-
involved in post-transcriptional tRNA modification
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
DELTAD-arm
-
tRNAPhe variant from yeast with a modification in the D-stem, inhibition
-
G18A
-
tRNAPhe variant from yeast with an exchange of G to A at position 18, inhibition
-
Polyamine
higher concentrations of linear polyamines inhibit TrmH activity at 55°C, while optimum concentration increases TrmH activity at 45-75°C
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
caldohexamine
1 mM caldohexamine increases TrmH activity at 60-80°C. No positive effect on the TrmH activity at 55°C
Polyamine
higher concentrations of linear polyamines inhibit TrmH activity at 55°C, while optimum concentration increases TrmH activity at 45-75°C
-
S-adenosyl-L-methionine
-
enhances the affinity for tRNA and induces formation of the tetramer structure
tetrakis(3-aminopropyl)ammonium
0.25 mM, increases TrmH activity at 40-85°C
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000082
guanosine18 in yeast tRNAPhe mutant transcript
-
pH and temperature not specified in the publication, Vmax: 3.1 micromol/mg/h
-
0.0125
guanosine18 in yeast tRNAPhe-AGA mutant transcript
-
pH and temperature not specified in the publication, Vmax: 0.00675 micromol/mg/h
-
0.00082
guanosine18 in yeast tRNAPhe-dG18 mutant transcript
-
pH and temperature not specified in the publication, Vmax: 0.1 micromol/mg/h
-
0.0002
guanosine18 in yeast tRNAPhe-GAA mutant transcript
-
pH and temperature not specified in the publication, Vmax: 0.135 micromol/mg/h
-
0.000245
guanosine18 in yeast tRNAPhe-GGA mutant transcript
-
pH and temperature not specified in the publication, Vmax: 1.2 micromol/mg/h
-
0.0003
guanosine18 in yeast tRNAPhe-GUA mutant transcript
-
pH and temperature not specified in the publication, Vmax: 0.18 micromol/mg/h
-
additional information
additional information
-
overview: Km of 28 tRNAPhe variants from yeast
-
0.00011
guanosine18 in yeast tRNAPhe
Q9FAC4
mutant E182A, pH not specified in the publication, temperature not specified in the publication
-
0.00012
guanosine18 in yeast tRNAPhe
Q9FAC4
mutant D180A, pH not specified in the publication, temperature not specified in the publication
-
0.00012
guanosine18 in yeast tRNAPhe
Q9FAC4
mutant Q185A, pH not specified in the publication, temperature not specified in the publication
-
0.00014
guanosine18 in yeast tRNAPhe
Q9FAC4
mutant V187A, pH not specified in the publication, temperature not specified in the publication
-
0.00015
guanosine18 in yeast tRNAPhe
Q9FAC4
wild-type, pH not specified in the publication, temperature not specified in the publication
-
0.00016
guanosine18 in yeast tRNAPhe
Q9FAC4
mutant K186A, pH not specified in the publication, temperature not specified in the publication
-
0.00026
guanosine18 in yeast tRNAPhe
Q9FAC4
mutant Y184A, pH not specified in the publication, temperature not specified in the publication
-
0.0013
guanosine18 in yeast tRNAPhe
Q9FAC4
mutant D190A, pH not specified in the publication, temperature not specified in the publication
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
65
additional information
-
optimal temperature for methylation is ca. 20°C lower than the melting temperature of the tRNA, overview
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 80
-
strain HB 8 shows 80% activity at 40°C, strain HB 27 shows 60% activity
52 - 79
-
at 67°C content of the TrmH protein is ca. 1/5000 of the total proteins, content of the TrmH protein in 52°C cultured cells slightly decreases as compared with that in 67°C cultured cells, TrmH contents in cells cultured at 75 or 79°C are similar to that at 67°C
55 - 75
-
about half-maximal activity at 55°C and 75°C, Escherichia coli tRNAfMet
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
21000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
-
in the absence of S-adenosyl-L-methionine or S-adenosyl-L-homocysteine
monomer
tetramer
monomer
-
addition of S-adenosyl-L-homocysteine causes the dissociation of subunits and gives rise to a monomer structure
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E124A
-
extensive structural alterations compared to wild-type, marked decrease in activity
H71A
-
has increased affinity for S-adenosyl-L-methionine, decreased affinity for tRNA
K32A
-
no change of affinity for S-adenosyl-L-methionine, decreased affinity for tRNA
K90A
-
no change of affinity for S-adenosyl-L-methionine, decreased affinity for tRNA
L179Stop
-
no change of affinity for S-adenosyl-L-methionine, markedly decreased affinity for tRNA
N152A
-
extensive structural alterations compared to wild-type, marked decrease in activity
N35D
-
marked decrease in Km-value for tRNA, low affinity for S-adenosyl-L-homocysteine
R109A
-
no change of affinity for S-adenosyl-L-methionine and slightly increased affinity for tRNA
R11A
-
has lost its affinity for S-adenosyl-L-methionine, decreased affinity for tRNA
R14M
-
dissociation of subunits consistent with that from the wild-type enzyme
R166A
-
no change of affinity for S-adenosyl-L-methionine, decreased affinity for tRNA
R168A
-
no change of affinity for S-adenosyl-L-methionine, decreased affinity for tRNA
R176A
-
no change of affinity for S-adenosyl-L-methionine, decreased affinity for tRNA
R19A
-
no change of affinity for S-adenosyl-L-methionine, decreased affinity for tRNA
R8A
-
no change of affinity for S-adenosyl-L-methionine, decreased affinity for tRNA
additional information
additional information
Q9FAC4
chimeric proteins of Escherichia coli and Thermus thermophilus enzymes demonstrate that the catalytic domain discriminates substrate tRNAs from nonsubstrate tRNAs. The N- and C-terminal regions do not function in the substrate tRNA discrimination process. The C-terminal region works in the initial binding process, in which nonsubstrate tRNA is not excluded, and structural movement of the motif 2 region of the catalytic domain in an induced-fit process is involved in substrate tRNA discrimination
additional information
-
chimeric proteins of Escherichia coli and Thermus thermophilus enzymes demonstrate that the catalytic domain discriminates substrate tRNAs from nonsubstrate tRNAs. The N- and C-terminal regions do not function in the substrate tRNA discrimination process. The C-terminal region works in the initial binding process, in which nonsubstrate tRNA is not excluded, and structural movement of the motif 2 region of the catalytic domain in an induced-fit process is involved in substrate tRNA discrimination
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
Thermus thermophilus strain HB27: 40% of maximal activity, strain HB8: 80% of maximal activity
80
80
-
about 90% of original activity retained after 20 min in the presence of 10% v/v glycerol at pH 7.5
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography on S-adenosyl-L-homocysteine-Sepharose, elution with 6 M urea
-
wild-type and mutants purified by gel filtration, mutants R11A and R166A purified by repeated ion-exchange chromatography, to homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli with and without His-tag, amino acid sequence analysis and comparison
Q9FAC4
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
medicine
-
in vitro methylation of immunostimulatory Gm18-negative tRNA with recombinant trmH from Thermus thermophilus abolishes its interferon-alpha-inducing potential
analysis
-
Arg-41 is the catalytic center, Lys-90, Arg-166, Arg-168, and Arg-176 are the initial sites of tRNA binding, Arg-8, Arg-19, and Lys-32 are required in the tRNA binding site for continuation the catalytic cycle, Arg-11-His-71-Met-147 interaction is involved in the structural element in release of S-adenosyl-L-homocysteine, His-34 plays a role in the assisted phosphate binding site, Arg-109 has an unknown function
analysis
-
dissociation of tRNA from the tRNA-enzyme complex after the methyl-transfer reaction is caused by the dissociation of enzyme subunits
analysis
-
through the log phase, the content of the TrmH protein is not changed obviously, but in the stationary phase, the content of the TrmH protein is slowly reduced
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kumagai, I.; Watanabe, K.; Oshima, T.
A thermostable tRNA (guanosine-2)-methyltransferase from Thermus thermophilus HB27 and the effect of ribose methylation on the conformational stability of tRNA
J. Biol. Chem.
257
7388-7395
1982
Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Matsumoto, T.; Watanabe, K.; Ohta, T.
Recognition mechanism of tRNA with tRNA(guanosine-2)methyltransferase from Thermus thermophilus HB 27
Nucleic Acids Symp. Ser.
15
131-134
1984
Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
Hori, H.; Matsumoto, T.; Watanabe, K.; Ohta, T.; Miura, K.
Two types of tRNA(Gm)methylase found in extreme thermophile, Thermus thermophilus strains HB 8 and HB 27
Nucleic Acids Symp. Ser.
16
225-228
1985
Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
Matsumoto, T.; Ohta, T.; Kumagai, I.; Oshima, T.; Murao, K.; Hasegawa, T.; Ishikura, H.; Watanabe, K.
A thermostable Gm-methylase recognizes the tertiary structure of tRNA
J. Biochem.
101
1191-1198
1987
Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Matsumoto, T.; Nishikawa, K.; Hori, H.; Ohta, T.; Miura, K.; Watanabe, K.
Recognition sites of tRNA by a thermostable tRNA(guanosine-2-)-methyltransferase from Thermus thermophilus HB27
J. Biochem.
107
331-338
1990
Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Hori, H.; Yamazaki, N.; Matsumoto, T.; Watanabe, Y.I.; Ueda, T.; Nishikawa, K.; Kumagai, I.; Watanabe, K.
Substrate recognition of tRNA (guanosine-2'-)-methyltransferase from Thermus thermophilus HB27
J. Biol. Chem.
273
25721-25727
1998
Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Hori, H.; Yamazaki, N.; Matsumoto, T.; Ueda, T.; Nishikawa, K.; Izumi, K.; Watanabe, K.
Essentially minimal sequence for substrate recognition by tRNA (guanosine-2')-methyltransferase from Thermus thermophilus HB27
Nucleic Acids Symp. Ser.
37
189-190
1997
Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
Hori, H.; Suzuki, T.; Sugawara, K.; Inoue, Y.; Shibata, T.; Kuramitsu, S.; Yokoyama, S.; Oshima, T.; Watanabe, K.
Identification and characterization of tRNA (Gm18) methyltransferase from Thermus thermophilus HB8: domain structure and conserved amino acid sequence motifs
Genes Cells
7
259-272
2002
Thermus thermophilus (Q9FAC4), Thermus thermophilus
Watanabe, K.; Nureki, O.; Fukai, S.; Ishii, R.; Okamoto, H.; Yokoyama, S.; Endo, Y.; Hori, H.
Roles of conserved amino acid sequence motifs in the SpoU (TrmH) RNA methyltransferase family
J. Biol. Chem.
280
10368-10377
2005
Thermus thermophilus
Nureki, O.; Watanabe, K.; Fukai, S.; Ishii, R.; Endo, Y.; Hori, H.; Yokoyama, S.
Deep knot structure for construction of active site and cofactor binding site of tRNA modification enzyme
Structure
12
593-602
2004
Thermus thermophilus (Q9FAC4)
Watanabe, K.; Nureki, O.; Fukai, S.; Endo, Y.; Hori, H.
Functional categorization of the conserved basic amino acid residues in TrmH (tRNA (Gm18) methyltransferase) enzymes
J. Biol. Chem.
281
34630-34639
2006
Thermus thermophilus
Watanabe, K.; Nureki, O.; Fukai, S.; Endo, Y.; Hori, H.
Structural change of tRNA (Gm18) methyltransferase by binding of methyl donor analogues
Nucleic Acids Symp. Ser.
49
301-302
2005
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Iwashita, C.; Hori, H.
Amount changes of tRNA modification enzymes in Thermus thermophilus HB8 cells according to culture temperatures
Nucleic Acids Symp. Ser.
50
247-248
2006
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Ochi, A.; Makabe, K.; Kuwajima, K.; Hori, H.
Flexible recognition of the tRNA G18 methylation target site by TrmH methyltransferase through first binding and induced fit processes
J. Biol. Chem.
285
9018-9029
2010
Thermus thermophilus
Ochi, A.; Makabe, K.; Yamagami, R.; Hirata, A.; Sakaguchi, R.; Hou, Y.M.; Watanabe, K.; Nureki, O.; Kuwajima, K.; Hori, H.
The catalytic domain of topological knot tRNA methyltransferase (TrmH) discriminates between substrate tRNA and nonsubstrate tRNA via an induced-fit process
J. Biol. Chem.
288
25562-25574
2013
Escherichia coli, Thermus thermophilus (Q9FAC4), Thermus thermophilus
Joeckel, S.; Nees, G.; Sommer, R.; Zhao, Y.; Cherkasov, D.; Hori, H.; Ehm, G.; Schnare, M.; Nain, M.; Kaufmann, A.; Bauer, S.
The 2-O-methylation status of a single guanosine controls transfer RNA-mediated Toll-like receptor 7 activation or inhibition
J. Exp. Med.
209
235-241
2012
Escherichia coli, Thermus thermophilus
Hori, H.; Terui, Y.; Nakamoto, C.; Iwashita, C.; Ochi, A.; Watanabe, K.; Oshima, T.
Effects of polyamines from Thermus thermophilus, an extreme-thermophilic eubacterium, on tRNA methylation by tRNA (Gm18) methyltransferase (TrmH)
J. Biochem.
159
509-517
2016
Thermus thermophilus (Q5SM16), Thermus thermophilus, Thermus thermophilus DSM 579 (Q5SM16)
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