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2 S-adenosyl-L-methionine + adenine58 in tRNA
2 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
2 S-adenosyl-L-methionine + adenine58 in tRNALys3
2 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNALys3
S-adenosyl-L-methionine + adenine58 in human tRNA3Lys
S-adenosyl-L-homocysteine + N1-methyladenine58 in human tRNA3Lys
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-
-
?
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 tRNA3Lys
S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA3Lys
-
-
-
?
S-adenosyl-L-methionine + adenine58 in tRNAGGUThr
S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
S-adenosyl-L-methionine + adenine58 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNAPhe
S-adenosyl-L-methionine + adenine58 in yeast initiator tRNAMet
S-adenosyl-L-homocysteine + N1-methyladenine58 in yeast initiator tRNAMet
no methylation of the A58U mutant of yeast initiator tRNA(Met)
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-
?
2 S-adenosyl-L-methionine + adenine58 in tRNA
2 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
-
-
-
?
2 S-adenosyl-L-methionine + adenine58 in tRNA
2 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
-
-
-
?
2 S-adenosyl-L-methionine + adenine58 in tRNA
2 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
-
-
-
?
2 S-adenosyl-L-methionine + adenine58 in tRNALys3
2 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNALys3
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-
-
?
2 S-adenosyl-L-methionine + adenine58 in tRNALys3
2 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNALys3
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-
-
?
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
-
-
-
-
?
S-adenosyl-L-methionine + adenine58 in initiator tRNAMet
S-adenosyl-L-homocysteine + N1-methyladenine58 in initiator tRNAMet
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
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?
S-adenosyl-L-methionine + adenine58 in initiator tRNAMet
S-adenosyl-L-homocysteine + N1-methyladenine58 in initiator tRNAMet
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
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-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
modification at the conserved nucleotide 58 in the TCC loop
-
-
?
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
-
-
-
-
?
S-adenosyl-L-methionine + adenine58 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
-
specific for the A58 position. Rv2118p does not methylate other positions in tRNA to any significant extent
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
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
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-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
S-adenosyl-L-methionine + adenine58 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
catalyzes the sitespecific formation of m1A at position 58 of the T-loop of tRNA in the absence of any other complementary protein
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-
?
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
-
-
-
?
S-adenosyl-L-methionine + adenine58 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
catalyzes the sitespecific formation of m1A at position 58 of the T-loop of tRNA in the absence of any other complementary protein
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-
?
S-adenosyl-L-methionine + adenine58 in tRNAGGUThr
S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
the tRNA from Thermus thermophilus, that contains C60 instead of U60, is poorly methylated. Nucleoside analysis of tRNAGGUThr from the wild-type strain indicates that less than 50% of tRNAGGUThr contain m1A58
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-
?
S-adenosyl-L-methionine + adenine58 in tRNAGGUThr
S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
the tRNA from Thermus thermophilus, that contains C60 instead of U60, is poorly methylated. Nucleoside analysis of tRNAGGUThr from the wild-type strain indicates that less than 50% of tRNAGGUThr contain m1A58
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-
?
S-adenosyl-L-methionine + adenine58 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNAPhe
the Thermus thermophilus tRNAPhe transcript is methylated efficiently by the Thermus thermophilus enzyme, whereas the Saccharomyces cerevisiae tRNAPhe transcript is poorly methylated. Analysis of fourteen chimeric tRNA transcripts derived from these two tRNA reveals that enzyme TrmI recognized the combination of aminoacyl stem, variable region, and T-loop. TrmI methylates deltion transcripts still containing the aminoacyl stem, variable region, and T-arm. Positive sequence determinants are C56, purine 57, A58, and U60. Replacing A58 with inosine and 2-aminopurine completely abrogates methylation, demonstrating that the 6-amino group in A58 is recognized by enzyme TrmI
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-
?
S-adenosyl-L-methionine + adenine58 in tRNAPhe
S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNAPhe
the Thermus thermophilus tRNAPhe transcript is methylated efficiently by the Thermus thermophilus enzyme, whereas the Saccharomyces cerevisiae tRNAPhe transcript is poorly methylated. Analysis of fourteen chimeric tRNA transcripts derived from these two tRNA reveals that enzyme TrmI recognized the combination of aminoacyl stem, variable region, and T-loop. TrmI methylates deltion transcripts still containing the aminoacyl stem, variable region, and T-arm. Positive sequence determinants are C56, purine 57, A58, and U60. Replacing A58 with inosine and 2-aminopurine completely abrogates methylation, demonstrating that the 6-amino group in A58 is recognized by enzyme TrmI
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 S-adenosyl-L-methionine + adenine58 in tRNA
2 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
2 S-adenosyl-L-methionine + adenine58 in tRNALys3
2 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNALys3
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 tRNA3Lys
S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA3Lys
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-
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?
2 S-adenosyl-L-methionine + adenine58 in tRNA
2 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
-
-
-
?
2 S-adenosyl-L-methionine + adenine58 in tRNA
2 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
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-
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?
2 S-adenosyl-L-methionine + adenine58 in tRNA
2 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
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-
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?
2 S-adenosyl-L-methionine + adenine58 in tRNALys3
2 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNALys3
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?
2 S-adenosyl-L-methionine + adenine58 in tRNALys3
2 S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNALys3
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?
S-adenosyl-L-methionine + adenine58 in initiator tRNAMet
S-adenosyl-L-homocysteine + N1-methyladenine58 in initiator tRNAMet
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?
S-adenosyl-L-methionine + adenine58 in initiator tRNAMet
S-adenosyl-L-homocysteine + N1-methyladenine58 in initiator tRNAMet
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
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-
?
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
-
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
-
-
-
?
S-adenosyl-L-methionine + adenine58 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
-
modification at the conserved nucleotide 58 in the TCC loop
-
-
?
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
-
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
-
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
S-adenosyl-L-methionine + adenine58 in tRNA
S-adenosyl-L-homocysteine + N1-methyladenine58 in tRNA
-
-
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-
?
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
-
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?
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.
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.
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evolution
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comparative structural analysis of TrmIs from archea, prokaryota, and eukaryota, overview
evolution
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comparative structural analysis of TrmIs from archea, prokaryota, and eukaryota, overview
evolution
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comparative structural analysis of TrmIs from archea, prokaryota, and eukaryota, overview
evolution
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comparative structural analysis of TrmIs from archea, prokaryota, and eukaryota, overview
evolution
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comparative structural analysis of TrmIs from archea, prokaryota, and eukaryota, overview
evolution
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comparative structural analysis of TrmIs from archea, prokaryota, and eukaryota, overview
evolution
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comparative structural analysis of TrmIs from archea, prokaryota, and eukaryota, overview
evolution
the N1-methyladenosine residue at position 58 of tRNA is found in the three domains of life
evolution
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
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. In mitochondria, MTase Trmt61B forms a tetramer, presumed to resemble the homotetramers of TrmI proteins. In support of a similar structural arrangement between Trmt61B and TrmI, a phylogenetic analysis confirmed a bacterial origin of the human protein
evolution
the m1A58 modification occurs on (cyt)tRNAs from all three domains of life and further in (mt)tRNAs. The m1A58 MTases belong to the RFM methyltransferase superfamily, class I. In archaea and bacteria, the m1A58 MTases belong to the TrmI subfamily and function without complex partners
evolution
TRM61 is the eukaryotic homologue of the bacterial and archaeal m1A58 tRNA methyl-transferase TrmI. Evolutionary relationship between TRM6 and TRM61, overview
evolution
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TRM61 is the eukaryotic homologue of the bacterial and archaeal m1A58 tRNA methyl-transferase TrmI. Evolutionary relationship between TRM6 and TRM61, overview
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malfunction
inactivation of the Thermus thermophilus trmI gene results in a thermosensitive phenotype (growth defect at 80°C)
malfunction
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
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siRNA knockdown of either subunit of the m1A58-methyltransferase results in a slow-growth phenotype, and a marked increase in the amount of m1A58 hypomodified tRNAs. Most m1A58 hypomodified tRNAs can associate with polysomes in varying extents
malfunction
deletion of the MTase N1-methylation A58 in yeast produces non-viable cells
malfunction
the lack of m1A58 in human tRNALys3 has been shown to be crucial for reverse transcription fidelity and efficiency of retroviruses like HIV-1. The lack of m1A58 results in an abnormal tRNAi structure, guiding it for degradation. This might explain why exclusion of this MTase by siRNA-mediated knockdown gives rise to a slow-growth phenotype in human cells
malfunction
the lack of the enzyme forming m1A58 leads to thermosensitivity in bacterial tRNAs
malfunction
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inactivation of the Thermus thermophilus trmI gene results in a thermosensitive phenotype (growth defect at 80°C)
-
metabolism
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 (mt) 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
metabolism
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
methylation of A58 is critical for maintaining the stability of initiator tRNAMet in yeast
physiological function
role of the N1-methylation of tRNA adenosine-58 in adaptation of life to extreme temperatures
physiological function
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
-
N1-adenine58 methylation of initiator-tRNAMet is required for stabilizing this tRNA in human cells
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
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 at high temperatures
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 at high temperatures
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 at high temperatures
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 at high temperatures
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
-
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
m1A58 modification of tRNA3Lys also has a role in replication of HIV in humans, human tRNA3 Lys is the primer for reverse transcription of HIV, the 3' end is complementary to the primer-binding site on HIV RNA. The complementarity ends at the 18th base, A58, which in tRNA3 Lys is modified to remove Watson-Crick pairing. tRNA m1A58 methyltransferase methylates N1 of A58, which is buried in the TPsiC-loop of tRNA, from cofactor S-adenosyl-L-methionine. This conserved tRNA modification is essential for stability of initiator tRNA
physiological function
the N1-methyladenosine residue at position 58 of tRNA is found in the three domains of life, and contributes to the stability of the three-dimensional L-shaped tRNA structure. In thermophilic bacteria, this modificationis important for thermal adaptation, and is catalyzed by thetRNA m1A58 methyltransferase TrmI, using S-adenosyl-L-methionine as the methyl donor
physiological function
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
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. 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 f hydrogen bonds between the conserved adenines. In this network, A58 forms hydrogen bonds to A54 and A60
physiological function
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. The combination of m1A58 with two other post-transcriptional modifications (Gm18 and m5s2U54) increases the melting temperature of tRNAs from Thermus thermophilus by approximately 10°C compared to the unmodified transcript
physiological function
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
physiological function
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role of the N1-methylation of tRNA adenosine-58 in adaptation of life to extreme temperatures
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physiological function
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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
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additional information
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microarray method genomic approach to determine the presence of m1A58 hypomodified tRNAs, on the basis of their permissiveness in primer extension, in human cell lines, overview. A58 hypomodification affects stability and involvement of tRNAs in translation. No hypomodification of initiator-tRNAMet. The pattern of the m1A58 hypomodified tRNAs is similar in five human cell lines
additional information
m1A58 MTase is composed of two subunits, a catalytic component, Trm61, and an RNA-binding component, Trm6. tRNAs bind across the dimer interface such that Trm6 from the opposing heterodimer brings A58 into the active site of Trm61. T-loop and D-loop are splayed apart showing how A58, normally buried in tRNA, becomes accessible for modification, mechanisms of modifying internal sites in folded tRNA, overview. 2Fold related tRNAs bind across the tetramer interface, active site structure analysis. m1A58 MTase uses induced fit to access its target base
additional information
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m1A58 MTase is composed of two subunits, a catalytic component, Trm61, and an RNA-binding component, Trm6. tRNAs bind across the dimer interface such that Trm6 from the opposing heterodimer brings A58 into the active site of Trm61. T-loop and D-loop are splayed apart showing how A58, normally buried in tRNA, becomes accessible for modification, mechanisms of modifying internal sites in folded tRNA, overview. 2Fold related tRNAs bind across the tetramer interface, active site structure analysis. m1A58 MTase uses induced fit to access its target base
additional information
recognition of tRNA substrate and structure of the catalytic pocket, overview. The flexibility of the N-terminal domain that is probably important to bind tRNA. Role of residue Y78 in stabilizing the conformation of the A58 ribose needed to hold substrate adenosine in the active site, and central role of residue D170 in binding the amino moiety of S-adenosyl-L-methionine and the exocyclic amino group of adenine
additional information
catalytic mechanism of m1A58 specific RFM family member TrmI, overview. The conserved aspartate residue (Asp181) is essential for m1A58 MTase activity in Thermus thermophilus
additional information
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
additional information
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
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
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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
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recognition of tRNA substrate and structure of the catalytic pocket, overview. The flexibility of the N-terminal domain that is probably important to bind tRNA. Role of residue Y78 in stabilizing the conformation of the A58 ribose needed to hold substrate adenosine in the active site, and central role of residue D170 in binding the amino moiety of S-adenosyl-L-methionine and the exocyclic amino group of adenine
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additional information
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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
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?
x * 29000, recombinant enzyme, SDS-PAGE, x * 28700, about, sequence calculation
heterodimer
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
heterodimer
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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
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heterotetramer
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dimers of tightly assembled heterodimers, formed by TrmI-6 and TrmI-61 subunits, interactions and structure analysis, overview
heterotetramer
the eukaryotic complex of Trm6-Trm61 has been reported as a heterotetramer
heterotetramer
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
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
heterotetramer
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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
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homotetramer
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4 * 31000, SDS-PAGE
homotetramer
bacterial and archaeal TrmI proteins have been shown to form homotetramers. Each homotetramers accomodates up to two tRNA molecules
tetramer
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dimers of tightly assembled dimers, hyperthermophilic enzymes present additional hydrophobic contacts at the dimer interfaces, interactions and structure analysis, overview
tetramer
dimer of heterodimers in which each heterodimer comprises a catalytic chain, Trm61, and a homologous but noncatalytic chain, Trm6, repurposed as a tRNA-binding subunit that acts in trans, crystal structure analysis
tetramer
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dimers of tightly assembled dimers, interactions and structure analysis, overview
tetramer
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dimers of tightly assembled dimers, hyperthermophilic enzymes present additional hydrophobic contacts at the dimer interfaces, and the tetramer is strengthened by four intersubunit disulfide bridges, interactions and structure analysis, overview
tetramer
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dimers of tightly assembled dimers, interactions and structure analysis, overview
tetramer
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dimers of tightly assembled dimers, bacterial enzymes from thermophilic organisms display additional intermolecular ionic interactions across the dimer interfaces, interactions and structure analysis, overview
tetramer
4 * 28582, calculation from sequence, composed of two types of subunits (Gcd14p and Gcd10p)
tetramer
the enzyme remains tetrameric upon tRNA binding, with formation of complexes involving one to two molecules of tRNA per TrmI tetramer
tetramer
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dimers of tightly assembled dimers, bacterial enzymes from thermophilic organisms display additional intermolecular ionic interactions across the dimer interfaces, interactions and structure analysis, overview
tetramer
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4 * 28582, calculation from sequence, composed of two types of subunits (Gcd14p and Gcd10p)
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additional information
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comparative structural analysis of TrmIs, overview
additional information
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comparative structural analysis of TrmIs, overview
additional information
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two subunit types, TRM6 or TRM61
additional information
Trm6 is less conserved with respect to TrmI than Trm61 and lacks a cofactor-binding pocket, enzyme quaternary structure, overview
additional information
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Trm6 is less conserved with respect to TrmI than Trm61 and lacks a cofactor-binding pocket, enzyme quaternary structure, overview
additional information
in mitochondria, MTase Trmt61B forms a tetramer, presumed to resemble the homotetramers of TrmI proteins. In support of a similar structural arrangement between Trmt61B and TrmI, a phylogenetic analysis confirmed a bacterial origin of the human protein
additional information
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comparative structural analysis of TrmIs, overview
additional information
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comparative structural analysis of TrmIs, overview
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
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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
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comparative structural analysis of TrmIs, overview
additional information
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comparative structural analysis of TrmIs, overview
additional information
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comparative structural analysis of TrmIs, overview
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purified enzyme in complex with S-adenosyl-L-methionine, sitting drop vapor diffusion method, mixing of 0.001 ml of 10-12 mg/ml protein in 20 mM Tris-HCl buffer, pH 8.0, containing 150 mM NaCl, 1 mM DTT, and 2 mM S-adenosyl-L-methionine, with 0.001 ml of reservoir solution containing 0.1 M Tris-HCl buffer, pH 8.4, and 20% ethanol, at 20°C, cryoprotection in 0.1 M Tris-HCl buffer, pH 8.4, 20% ethanol, and 35% ethylene glycol, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular replacement method, using the coordinates of TrmI from Thermotoga maritima, PDB ID 1O54, as the starting model
TrmI complexed with S-adenosyl-L-methionine, X-ray diffraction structure determination and analysis at 2.2 A resolution
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crystal structure of the human m1A58 MTase in complex with tRNALys3 (PDB ID 5CCB), and of human complex Trm6-Trm61 (PDB ID 2B25)
human enzyme tRNA m1A58 MTase in complex with human tRNA3Lys and cofactors S-adenosyl-L-methionine or S-adenosyl-L-homocysteine, hanging drop vapor diffusion method, mixing of 0.001 ml of 4.8 mg/ml protein in 50 mM HEPES, pH 7.5, 0.0664 mM tRNA3Lys, 2 mM S-adenosyl-L-methionine or S-adenosyl-L-homocysteine, and 1 mM MgCl2, with 0.001 ml of reservoir solution containing 0.1 M Na acetate, pH 4.8-5.0, 2% w/v PEG 4000 and 15% v/v methyl-2,4-pentanediol, 16°C, 4-7 days, X-ray diffraction structure determination and analysis at 2.2-4.0 A resolution, molecular replacement
TrmI-61 protein complexed with S-adenosyl-L-methionine, X-ray diffraction structure determination and analysis at 2.5 A resolution
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crystal structure of Rv2118c in complex with S-adenosyl-L-methionine has been determined at 1.98 A resolution
TrmI complexed with S-adenosyl-L-methionine, X-ray diffraction structure determination and analysis at 1.98 A resolution
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TrmI protein complexed as tetramer with S-adenosyl-L-homocysteine or as monomer with S-adenosyl-L-methionine, X-ray diffraction structure determination and analysis at 2.05-2.6 A or 1.6 A resolution, respectively
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crystal structure is available for heterotetrameric Trm6-Trm61A complex from Saccharomyces cerevisiae
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
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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
ligand-free TrmI, X-ray diffraction structure determination and analysis at 1.65 A resolution
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purified enzyme mutant D170A and Y78A in complex with S-adenosyl-L-methionine, hanging drop vapor diffusion method, mixing of 10 mg/ml protein in 20 mM Tris-HCl buffer, pH 8.0, 100 mM KCl, and 2mM S-adenosyl-L-methionine with reservoir solution containing 2.4 M ammonium sulfate and 10% v/v isopropanol for mutant D170A and 2.1 M ammonium sulfate and 8% v/v isopropanol for mutant Y78A, X-ray diffraction structure determination and analysis at 3.1 A and 2.6 A resolution, respectively. Crystallization assays of enzyme TrmI Y194A lead to poorly diffracting crystals
sitting-drop vapor-diffusion method at 19°C. Crystal structure of TrmI, in complex with S-adenosyl-L-homocysteine, is determined at 1.7 A resolution. The conserved residues that form the catalytic cavity (D170, Y78, and Y194) are essential for fashioning an optimized shape of the catalytic pocket
TrmI protein complexed with S-adenosyl-L-homocysteine, X-ray diffraction structure determination and analysis at 1.7 A resolution
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D170A
site-directed mutagenesis, mutation of a conserved active site residue
Y194A
site-directed mutagenesis, crystallization assays of TrmI Y194A lead to poorly diffracting crystals
Y78A
site-directed mutagenesis, mutation of a conserved active site residue. The structure of TrmI Y78A catalytic domain is unmodified regarding the binding of the SAM co-factor and the conformation of residues potentially interacting with the substrate adenine, as compared to the wild-type structure. The structure of the D170A mutant shows a flexible active site with one loop occupying in part the place of the co-factor and the second loop moving at the entrance to the active site
D170A
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site-directed mutagenesis, mutation of a conserved active site residue
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Y194A
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site-directed mutagenesis, crystallization assays of TrmI Y194A lead to poorly diffracting crystals
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Y78A
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site-directed mutagenesis, mutation of a conserved active site residue. The structure of TrmI Y78A catalytic domain is unmodified regarding the binding of the SAM co-factor and the conformation of residues potentially interacting with the substrate adenine, as compared to the wild-type structure. The structure of the D170A mutant shows a flexible active site with one loop occupying in part the place of the co-factor and the second loop moving at the entrance to the active site
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additional information
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siRNA knockdown of m1A58 methyltransferase subunits TRM6 or TRM61
additional information
mutations in the predicted AdoMet-binding domain destroyed GCD14 function in vivo and (m1A)MTase activity in vitro
additional information
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mutations in the predicted AdoMet-binding domain destroyed GCD14 function in vivo and (m1A)MTase activity in vitro
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
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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 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
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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
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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
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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
brenda
Droogmans, L.; Roovers, M.; Bujnicki, J.M.; Tricot, C.; Hartsch, T.; Stalon, V.; Grosjean, H.
Cloning and characterization of tRNA (m1A58) methyltransferase (TrmI) from Thermus thermophilus HB27, a protein required for cell growth at extreme temperatures
Nucleic Acids Res.
31
2148-2156
2003
Thermus thermophilus (Q8GBB2), Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 (Q8GBB2)
brenda
Varshney, U.; Ramesh, V.; Madabushi, A.; Gaur, R.; Subramanya, H.S.; RajBhandary, U.L.
Mycobacterium tuberculosis Rv2118c codes for a single-component homotetrameric m1A58 tRNA methyltransferase
Nucleic Acids Res.
32
1018-1027
2004
Mycobacterium tuberculosis
brenda
Barraud, P.; Golinelli-Pimpaneau, B.; Atmanene, C.; Sanglier, S.; Van Dorsselaer, A.; Droogmans, L.; Dardel, F.; Tisne, C.
Crystal structure of Thermus thermophilus tRNA m1A58 methyltransferase and biophysical characterization of its interaction with tRNA
J. Mol. Biol.
377
535-550
2008
Thermus thermophilus (Q8GBB2), Thermus thermophilus
brenda
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
brenda
Gupta, A.; Kumar, P.H.; Dineshkumar, T.K.; Varshney, U.; Subramanya, H.S.
Crystal structure of Rv2118c: an AdoMet-dependent methyltransferase from Mycobacterium tuberculosis H37Rv
J. Mol. Biol.
312
381-391
2001
Mycobacterium tuberculosis (P9WFZ1), Mycobacterium tuberculosis H37Rv (P9WFZ1), Mycobacterium tuberculosis H37Rv
brenda
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
brenda
Ozanick, S.; Krecic, A.; Andersland, J.; Anderson, J.T.
The bipartite structure of the tRNA m1A58 methyltransferase from S. cerevisiae is conserved in humans
RNA
11
1281-1290
2005
Homo sapiens (Q96FX7 and Q9UJA5), Homo sapiens
brenda
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
brenda
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, Saccharomyces cerevisiae, Thermus thermophilus, Homo sapiens, Mycobacterium tuberculosis, Pyrococcus abyssi, Thermotoga maritima
brenda
Saikia, M.; Fu, Y.; Pavon-Eternod, M.; He, C.; Pan, T.
Genome-wide analysis of N1-methyl-adenosine modification in human tRNAs
RNA
16
1317-1327
2010
Homo sapiens
brenda
Degut, C.; Ponchon, L.; Folly-Klan, M.; Barraud, P.; Tisne, C.
The m1A58 modification in eubacterial tRNA: An overview of tRNA recognition and mechanism of catalysis by TrmI
Biophys. Chem.
210
27-34
2016
Thermus thermophilus (Q8GBB2), Thermus thermophilus DSM 7039 (Q8GBB2)
brenda
Takuma, H.; Ushio, N.; Minoji, M.; Kazayama, A.; Shigi, N.; Hirata, A.; Tomikawa, C.; Ochi, A.; Hori, H.
Substrate tRNA recognition mechanism of eubacterial tRNA (m1A58) methyltransferase (TrmI)
J. Biol. Chem.
290
5912-5925
2015
Thermus thermophilus (Q8GBB2), Thermus thermophilus, Thermus thermophilus DSM 7039 (Q8GBB2)
brenda
Finer-Moore, J.; Czudnochowski, N.; OConnell, J.I.; Wang, A.; Stroud, R.
Crystal structure of the human tRNA m1A58 methyltransferase-tRNA3 Lys complex: Refolding of Substrate tRNA Allows Access to the Methylation Target
J. Mol. Biol.
427
3862-3876
2015
Homo sapiens (Q96FX7), Homo sapiens
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Kuratani, M.; Yanagisawa, T.; Ishii, R.; Matsuno, M.; Si, S.Y.; Katsura, K.; Ushikoshi-Nakayama, R.; Shibata, R.; Shirouzu, M.; Bessho, Y.; Yokoyama, S.
Crystal structure of tRNA m1A58 methyltransferase TrmI from Aquifex aeolicus in complex with S-adenosyl-L-methionine
J. Struct. Funct. Genomics
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173-180
2014
Aquifex aeolicus (O66653), Aquifex aeolicus
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Oerum, S.; Degut, C.; Barraud, P.; Tisne, C.
m1A Post-transcriptional modification in tRNAs
Biomolecules
7
20
2017
Saccharomyces cerevisiae (P41814 AND P46959), Thermus thermophilus (Q8GBB2), Homo sapiens (Q9UJA5 AND Q96FX7 AND Q9BVS5)
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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.
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32562
2016
Saccharomyces cerevisiae (P41814 AND P46959), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P41814 AND P46959)
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