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Information on EC 2.1.1.220 - tRNA (adenine58-N1)-methyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P46959
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2.1.1.220 tRNA (adenine58-N1)-methyltransferaseIUBMB Comments
The enzyme specifically methylates adenine58 in tRNA. The methylation of A58 is critical for maintaining the stability of initiator tRNAMet in yeast .
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Word Map
- 2.1.1.220
- trnaimet
- 1-methyladenosine
- nucleoside
- mtases
-
two-subunit
-
thermus
-
exosome
-
polyadenylation
- adomet
-
t-loop
- polya
- s-adenosylmethionine
-
n1-methylation
- heterotetramer
-
homotetrameric
- methionyl-trna
-
high-copy-number
- eubacteria
- methyltransferases
- s-adenosyl-l-homocysteine
-
two-component
-
s-adenosyl-l-methionine-dependent
-
l-shaped
-
tpsic
-
trna-binding
-
hypomodified
- drug development
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
+
adenine58 in tRNA
=
+
N1-methyladenine58 in tRNA
Synonyms
gcd14p, gcd10p, rv2118c, trna m(1)a58 methyltransferase, rv2118p, trm61p, trm6p, trm6-trm61 holoenzyme, trna (m1a58) methyltransferase, m1a58 trna methyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
m1A58 MTase
TrmI
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + adenine58 in tRNA = S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
TRM61 is the subunit that binds S-adenosyl-l-methionine and both subunits contribute to target tRNA binding, catalytic mechanism, overview
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNA (adenine58-N1)-methyltransferase
The enzyme specifically methylates adenine58 in tRNA. The methylation of A58 is critical for maintaining the stability of initiator tRNAMet in yeast [3].
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
2 S-adenosyl-L-methionine + adenine58 in tRNA
2 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
P41814; P46959
-
-
-
?
2 S-adenosyl-L-methionine + adenine58 in tRNALys3
2 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNALys3
P41814; P46959
-
-
-
?
S-adenosyl-L-methionine + adenine58 in initiator tRNAMet
S-adenosyl-L-homocysteine + N1-methyladenine58 in initiator tRNAMet
S-adenosyl-L-methionine + adenine58 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
S-adenosyl-L-methionine + adenine58 in initiator tRNAMet
S-adenosyl-L-homocysteine + N1-methyladenine58 in initiator tRNAMet
P46959; P41814
-
-
-
?
S-adenosyl-L-methionine + adenine58 in initiator tRNAMet
S-adenosyl-L-homocysteine + N1-methyladenine58 in initiator tRNAMet
-
-
-
-
?
S-adenosyl-L-methionine + adenine58 in initiator tRNAMet
S-adenosyl-L-homocysteine + N1-methyladenine58 in initiator tRNAMet
P46959; P41814
the Gcd10pGcd14p complex is required specifically at the initiation step of translation because of a strong requirement for 1-methyladenosine at position 58 (m1A58) in the processing and accumulation of initiator tRNAMet
-
-
?
S-adenosyl-L-methionine + adenine58 in initiator tRNAMet
S-adenosyl-L-homocysteine + N1-methyladenine58 in initiator tRNAMet
P46959; P41814
purified Flag-tagged Gcd14p alone had no enzymatic activity and is severely impaired for tRNA-binding compared with the wild-type complex, suggesting that Gcd10p is required for tight binding of the tRNA substrate
-
-
?
S-adenosyl-L-methionine + adenine58 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
-
-
-
-
?
S-adenosyl-L-methionine + adenine58 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
P41814; P46959
-
-
-
?
S-adenosyl-L-methionine + adenine58 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
-
TRM6 and TRM61 which compose a tRNA m1A58 methyltransferase that methylates m1A58 in tRNAs, especially tRNAiMe
-
-
?
S-adenosyl-L-methionine + adenine58 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
-
tRNA m1A58 methyltransferase, TrmI, catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to N1 of adenine 58 in the T-loop of tRNAs
-
-
?
S-adenosyl-L-methionine + adenine58 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
-
adenine at position 58 is the most conserved nucleoside in tRNA and is located in the TpsiC loop
-
-
?
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
2 S-adenosyl-L-methionine + adenine58 in tRNA
2 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
P41814; P46959
-
-
-
?
2 S-adenosyl-L-methionine + adenine58 in tRNALys3
2 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNALys3
P41814; P46959
-
-
-
?
S-adenosyl-L-methionine + adenine58 in initiator tRNAMet
S-adenosyl-L-homocysteine + N1-methyladenine58 in initiator tRNAMet
S-adenosyl-L-methionine + adenine58 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
S-adenosyl-L-methionine + adenine58 in initiator tRNAMet
S-adenosyl-L-homocysteine + N1-methyladenine58 in initiator tRNAMet
P46959; P41814
-
-
-
?
S-adenosyl-L-methionine + adenine58 in initiator tRNAMet
S-adenosyl-L-homocysteine + N1-methyladenine58 in initiator tRNAMet
P46959; P41814
the Gcd10pGcd14p complex is required specifically at the initiation step of translation because of a strong requirement for 1-methyladenosine at position 58 (m1A58) in the processing and accumulation of initiator tRNAMet
-
-
?
S-adenosyl-L-methionine + adenine58 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
P41814; P46959
-
-
-
?
S-adenosyl-L-methionine + adenine58 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
-
TRM6 and TRM61 which compose a tRNA m1A58 methyltransferase that methylates m1A58 in tRNAs, especially tRNAiMe
-
-
?
S-adenosyl-L-methionine + adenine58 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
-
tRNA m1A58 methyltransferase, TrmI, catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to N1 of adenine 58 in the T-loop of tRNAs
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-adenosyl-L-methionine
P41814; P46959
SAM is situated in a cleft on the surface of the C-terminal Rossmann-fold domain of TRM61. The interaction between TRM61 and SAM can be divided into three parts in accordance to the moieties of SAM. For the adenine moiety, the side-chain atom OD1 of Asp168 makes a hydrogen bond with the nitrogen N6 of the adenine. Modeling of the SAM binding site and a possible adenine-binding pocket of TRM6-TRM61
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000025
adenine58 in initiator tRNAMet
P46959; P41814
pH 8.0, 30°C, purified FlagGcd10pyGcd14p complex
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
P46959: subunit Gcd14p (catalytic subunit), P41814: subunit Gcd10p (non-catalytic subunit)
P46959; P41814
SwissProt
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
P41814; P46959
in cytosolic (cyt) tRNA, the m1A modification occurs at five different positions (9, 14, 22, 57, and 58), two of which (9 and 58) are also found in mitochondrial tRNAs. In some cases, these modifications have been shown to increase tRNA structural stability and induce correct tRNA folding. Two enzyme families are responsible for formation of m1A at nucleotide position 9 and 58 in tRNA, tRNA binding, m1A mechanism, protein domain organisation and overall structures
physiological function
additional information
evolution
-
comparative structural analysis of TrmIs from archea, prokaryota, and eukaryota, overview
evolution
P41814; P46959
the m1A58 modification occurs on (cyt)tRNAs from all three domains of life and further in (mt)tRNAs. The enzyme belongs to the RFM class I methyltransferases. In eukaryotes, the m1A58 MTase located in the cytosol is composed of a catalytic protein unit from the Trm61 subfamily (Trm61A) and an RNA-binding protein unit from the Trm6 subfamily (Trm6). Trm6 and Trm61 share a common ancestor and arose via gene duplication and divergent evolution. The mitochondrial m1A58 MTase consists of a single protein from the Trm61 family (Trmt61B), which is a paralogue to Trm61A from the cytosolic complex
evolution
P41814; P46959
TRM61 is the eukaryotic homologue of the bacterial and archaeal m1A58 tRNA methyl-transferase TrmI. Evolutionary relationship between TRM6 and TRM61, overview
malfunction
P46959; P41814
the absence of m1A from all tRNAs in Saccharomyces cerevisiae mutants lacking Gcd10p elicits severe defects in processing and stability of initiator methionine tRNA
malfunction
P41814; P46959
deletion of the MTase N1-methylation A58 in yeast produces non-viable cells
physiological function
P46959; P41814
the Gcd10pGcd14p complex is required specifically at the initiation step of translation because of a strong requirement for 1-methyladenosine at position 58 (m1A58) in the processing and accumulation of initiator tRNAMet
physiological function
-
TRM6 and TRM61 compose a tRNA methyltransferase which catalyzes the methylation of the N1 of adenine at position 58 in tRNAs, especially initiator methionine tRNA. The TRM6-TRM61 complex is required specifically in the initiation step of translation because of a strong requirement for m1A58 in the processing and accumulation of tRNAiMet. It is also required for repression of translation of GCN4, a gene encoding a transcriptional activator of amino-acid biosynthetic enzymes, mRNA
physiological function
-
tRNA m1A58 methyltransferase catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to N1 of adenine 58 in the T-loop of tRNAs, a modification, that is essential for cell growth in yeast
physiological function
P41814; P46959
the m1A58 modifications have both been linked to structural stability and/or correct folding of the tRNA and is related to structural thermostability of tRNA, role of m1A58 in tRNAi structure stability. m1A58 is important for maturation of the initiator tRNAMet from yeast. The initiator tRNA from eukaryotes (tRNAi) has a conserved A-rich T-loop (A54, A58, and A69), a conserved A20 and a shorter-than-average D-loop (seven nucleobases). These features cluster in the corner of the L-shaped tRNA and the structure is maintained by a dense network of hydrogen bonds between the conserved adenines. In this network, A58 forms hydrogen bonds to A54 and A60
physiological function
P41814; P46959
the N1 methylation of adenine at position 58 (m1A58) of tRNA is an important post-transcriptional modification, which is vital for maintaining the stability of the initiator methionine tRNAiMet. Adenine at position 58 (A58) located in the T-loop is one of the most conserved nucleosides in tRNA. In eukaryotes, this modification is performed by the TRM6-TRM61 holoenzyme, molecular mechanism that underlies the cooperation of TRM6 and TRM61 in the methyl transfer reaction, overview
additional information
P41814; P46959
crystal structure of the human m1A58 MTase in complex with tRNALys3 have not provided information on the correct mechanism, as the position of A58 in the active site resembles a methylated nucleobase in a product-complex. tRNA undergoes large conformational changes during binding in which the D- and T-arm are separated. The T-loop contains the nucleobase to be modified (A58) and binds in the active site. The binding is stabilised by the formation of numerous hydrogen bonds with the C56 nucleobase and the sugar-phosphate backbone. A stabilising hydrogen bond is also formed between a phosphate O atom of C56 and a H atom of the exocyclic N6 atom of A58. No hydrogen bonds are observed between the protein complex and A58, and the orientation of this adenosine towards the bound S-adenosyl-L-homocysteine (SAH) resembles a methylated nucleobase. A conserved aspartate residue (Asp181) is found in close proximity to A58 and could serve as the catalytic base. The complex makes additional contacts with the tRNA substrate with binding of the acceptor stem to the N?terminal domain of the catalytic subunit Trm61, and binding of the T?stem/loop to an insert in the N?terminal domain of Trm6, not present in Trm61. The vast number of interactions with both complex subunits explain previous findings that both Trm6 and Trm61 are required for tRNA binding. The interactions between tRNA and Trm6 help orient A58 for catalysis and may contribute to target specificity, providing a role for the non?catalytic subunit Trm6 in activity
additional information
P41814; P46959
two TRM6-TRM61 heterodimers assemble as a heterotetramer. Both TRM6 and TRM61 subunits comprise an N-terminal beta-barrel domain linked to a C-terminal Rossmann-fold domain. TRM61 functions as the catalytic subunit, containing a methyl donor (SAM) binding pocket. TRM6 diverges from TRM61, lacking the conserved motifs used for binding SAM. TRM6 cooperates with TRM61 forming an L-shaped tRNA binding regions. Target tRNA recognition and catalytic mechanism of the two component m1A58 tRNA methyl-transferase, overview
additional information
-
two TRM6-TRM61 heterodimers assemble as a heterotetramer. Both TRM6 and TRM61 subunits comprise an N-terminal beta-barrel domain linked to a C-terminal Rossmann-fold domain. TRM61 functions as the catalytic subunit, containing a methyl donor (SAM) binding pocket. TRM6 diverges from TRM61, lacking the conserved motifs used for binding SAM. TRM6 cooperates with TRM61 forming an L-shaped tRNA binding regions. Target tRNA recognition and catalytic mechanism of the two component m1A58 tRNA methyl-transferase, overview
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). A0A8H4FC47_YEASX
383
0
43920
TrEMBL
other Location (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
P41814; P46959
TRM6 and TRM61 form a compact complex via numerous hydrogen bonding and extensive hydrophobic interactions. The heterodimer interface of TRM6-TRM61 buries 3194 A2 of TRM6 and 3167 A2 of TRM61 solvent-accessible area, which represents about 17% and 16% of TRM6 and TRM61's total surface area, respectively. TRM6 mainly interacts with TRM61 through four major sites. Interaction analyses for sites A-C, detailed overview
heterotetramer
tetramer
-
dimers of tightly assembled dimers, interactions and structure analysis, overview
additional information
heterotetramer
P41814; P46959
the eukaryotic complex of Trm6-Trm61 has been reported as a heterotetramer. In the complex of Trm6-Trm61 from Saccharomyces cerevisiae, both subunits harbour an N-terminal domain linked to a C-terminal domain. The C-terminal domains cover a Rossmann-fold and are very similar between the two subunits, whereas significant differences are found between the N-terminal domains. The N-terminal domain of Trm61 contains a short alpha-helix and three hairpin beta-motifs, whereas Trm6 consists of a short alpha-helix with seven antiparallel beta-strands and a highly flexible region with a number of positively-charged residues. Each subunit of the Trm6-Trm61 complex forms heterodimers that, again, assemble as a heterotetramer. The catalytic subunit of this complex (Trm61) binds the cofactor SAM, a binding that is made impossible in the other subunit (Trm6) by the loss of conserved motifs involved in accommodation of this cofactor. Each heterotetramer binds two tRNA molecules onto two distal, L-shaped surfaces on the protein complex
heterotetramer
P41814; P46959
two TRM6-TRM61 heterodimers assemble as a heterotetramer. A symmetric unit of the TRM6-TRM61 crystal contains one molecule of TRM6 and one molecule of TRM61, forming a 1:1 heterodimer. TRM6 and TRM61 form a 2:2 tetrameric heterocomplex, displaying an omega shape. Two symmetry-related TRM6-TRM61 heterodimer come together to form a central beta-barrel structure that consists of beta13 (TRM6), loop beta13/beta14 (TRM6), beta12(TRM61) and loop beta13/beta14 (TRM61). The top of the barrel contains a hydrophobic core, formed by residues Tyr422 (TRM6), Pro431 (TRM6), Met253 (TRM61), His354 (TRM61), and Tyr357 (TRM61) The center of the barrel is filled with numerous hydrophilic side-chains, including residues Glu416 (TRM6), Arg418 (TRM6), Arg420 (TRM6), Glu255 (TRM61), Gln257 (TRM61) and Arg259 (TRM61). The bottom of the barrel consists of a cage of four tyrosine residues. Modelling of the heterotetramer interface of TRM6-TRM61, overview. A TRM6-TRM61 heterotetramer constitutes two L-shaped tRNA binding regions. Structure comparison to the enzyme from Homo sapiens
additional information
P46959; P41814
Gcd10p and Gcd14p function directly in m1A formation in yeast tRNAs. Purified Gcd14p alone had no enzymatic activity and is defective for tRNA binding compared with the Gcd14pyGcd10p complex. Gcd10p is required for tight binding of the tRNA substrate
additional information
-
Gcd10p and Gcd14p function directly in m1A formation in yeast tRNAs. Purified Gcd14p alone had no enzymatic activity and is defective for tRNA binding compared with the Gcd14pyGcd10p complex. Gcd10p is required for tight binding of the tRNA substrate
additional information
-
comparative structural analysis of TrmIs, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure is available for heterotetrameric Trm6-Trm61A complex from Saccharomyces cerevisiae
P41814; P46959
purified recombinant His-tagged TRM6-TRM61 complex, from 0.1 M KCl, 0.1 M Tris-HCl, pH 8.0, 25% w/v PEG 2000 MME, X-ray diffraction structure determination and analysis at 2.8 A resolution, molecular replacement
-
purified recombinant wild-type and selenomethionine-labeled holoenzyme in apoform and complexed with S-adenosyl-L-methionine (SAM), mixing of 15 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 300 mM NaCl, and 5 mM DTT, with a three-fold molecular excess of S-adenosyl-L-methionine, sitting drop vapour diffusion method, with the mother liquor containing 0.1 M HEPES, PH 7.5, 2% v/v 2-methyl-2,4-pentanediol, 10% w/v PEG 6000, 3 days X-ray diffraction structure determination and analysis
P41814; P46959
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
P46959; P41814
mutations in the predicted AdoMet-binding domain destroyed GCD14 function in vivo and (m1A)MTase activity in vitro
additional information
-
mutations in the predicted AdoMet-binding domain destroyed GCD14 function in vivo and (m1A)MTase activity in vitro
additional information
P46959; P41814
the reduced m1A levels observed in vivo and the lack of Mtase activity seen in vitro result from the inability of trm6-416, trm6-420, trm6-504, trm61-255 and trm6-416/trm61-255 mutants to effectively bind their tRNA substrate
additional information
-
the reduced m1A levels observed in vivo and the lack of Mtase activity seen in vitro result from the inability of trm6-416, trm6-420, trm6-504, trm61-255 and trm6-416/trm61-255 mutants to effectively bind their tRNA substrate
additional information
P41814; P46959
the human homologue of the yeast tRNA m1A58 methyltransferase is identified through amino acid sequence identity and complementation of the yeast temperature-sensitive TRM6 andTRM61 mutant phenotypes27. When co-expressed in yeast, the Homo sapiens TRM6-TRM61 catalyzes the in vitro methyl transfer reaction for both the yeast initiator tRNAi Met and human tRNA3Lys27
additional information
-
the human homologue of the yeast tRNA m1A58 methyltransferase is identified through amino acid sequence identity and complementation of the yeast temperature-sensitive TRM6 andTRM61 mutant phenotypes27. When co-expressed in yeast, the Homo sapiens TRM6-TRM61 catalyzes the in vitro methyl transfer reaction for both the yeast initiator tRNAi Met and human tRNA3Lys27
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged TRM6 and TRM61 from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography and gel filtration
-
recombinant wild-type and selenomethionine-labeled His-tagged subunits Trm6 and Trm61 from Escherichia coli by nickel affinity chromatography and gel filtration
P41814; P46959
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
genes GCD10 and GCD14 encoding TRM6 and TRM61, expression of His-tagged proteins in Escherichia coli strain Rosetta (DE3)
-
genes GCD10 and GCD14, recombinant co-expression of wild-type and selenomethionine-labeled His-tagged subunits in Escherichia coli
P41814; P46959
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Anderson, J.; Phan, L.; Hinnebusch, A.G.
The Gcd10p/Gcd14p complex is the essential two-subunit tRNA(1-methyladenosine) methyltransferase of Saccharomyces cerevisiae
Proc. Natl. Acad. Sci. USA
97
5173-5178
2000
Saccharomyces cerevisiae (P46959 and P41814), Saccharomyces cerevisiae
Anderson, J.; Phan, L.; Cuesta, R.; Carlson, B.A.; Pak, M.; Asano, K.; Bjrk, G.R.; Tamame, M.; Hinnebusch, A.G.
The essential Gcd10p-Gcd14p nuclear complex is required for 1-methyladenosine modification and maturation of initiator methionyl-tRNA
Genes Dev.
12
3650-3662
1998
Saccharomyces cerevisiae (P46959 and P41814), Saccharomyces cerevisiae
Ozanick, S.G.
Bujnicki, J.M.; Sem, D.S.; Anderson, J.T.: Conserved amino acids in each subunit of the heteroligomeric tRNA m1A58 Mtase from Saccharomyces cerevisiae contribute to tRNA binding
Nucleic Acids Res.
35
6808-6819
2007
Saccharomyces cerevisiae (P46959 and P41814), Saccharomyces cerevisiae
Qiu, X.; Huang, K.; Ma, J.; Gao, Y.
Crystallization and preliminary X-ray diffraction crystallographic study of tRNA m1A58 methyltransferase from Saccharomyces cerevisiae
Acta Crystallogr. Sect. F
67
1448-1450
2011
Saccharomyces cerevisiae
Guelorget, A.; Barraud, P.; Tisne, C.; Golinelli-Pimpaneau, B.
Structural comparison of tRNA m(1)A58 methyltransferases revealed different molecular strategies to maintain their oligomeric architecture under extreme conditions
BMC Struct. Biol.
11
48
2011
Aquifex aeolicus, Homo sapiens, Mycobacterium tuberculosis, Pyrococcus abyssi, Saccharomyces cerevisiae, Thermotoga maritima, Thermus thermophilus
Oerum, S.; Degut, C.; Barraud, P.; Tisne, C.
m1A Post-transcriptional modification in tRNAs
Biomolecules
7
20
2017
Homo sapiens (Q9UJA5 AND Q96FX7 AND Q9BVS5), Saccharomyces cerevisiae (P41814 AND P46959), Thermus thermophilus (Q8GBB2)
Wang, M.; Zhu, Y.; Wang, C.; Fan, X.; Jiang, X.; Ebrahimi, M.; Qiao, Z.; Niu, L.; Teng, M.; Li, X.
Crystal structure of the two-subunit tRNA m(1)A58 methyltransferase TRM6-TRM61 from Saccharomyces cerevisiae
Sci. Rep.
6
32562
2016
Saccharomyces cerevisiae (P41814 AND P46959), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P41814 AND P46959)
EXTERNAL LINKS (specific for EC-Number 2.1.1.220)
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