Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
S-adenosyl-L-methionine + cytosine32 in tRNA1Ser
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Ser
S-adenosyl-L-methionine + cytosine32 in tRNA1Thr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Thr
S-adenosyl-L-methionine + cytosine32 in tRNASer
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNASer
S-adenosyl-L-methionine + cytosine32 in tRNAThr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr
S-adenosyl-L-methionine + cytosine32 in tRNAThr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr(CGU)
G35 and U36 of tRNAThr(CGU) are required for m3C formation. Trm140 specifically binds tRNAThr substrates, overview. Best tRNAThr substrate is tRNATyr(GUA), lower activity occurs with tRNAThr(CGU), tRNAThr(IGU), and tRNAThr(UGU)
-
-
?
additional information
?
-
S-adenosyl-L-methionine + cytosine32 in tRNA1Ser
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Ser
tRNASer1 = tRNASer(UGA). Because position 32 of tRNA has an important role in accurate codon recognition, N3-methylcytosine32 formation in tRNAThr1 or tRNASer1 might play a role in modulating codon recognition and translational efficiency
-
-
?
S-adenosyl-L-methionine + cytosine32 in tRNA1Ser
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Ser
tRNAThr1 = tRNAThr(IGU). ABP140 is identified as the protein responsible for N3-methylcytosine32 formation in both tRNAThr1 and tRNASer1 by systematic reverse genetic approach combined with mass spectrometry (ribonucleome analysis). N3-Methylcytosine32 formation in tRNAThr1 can be reconstituted using recombinant Abp140p in the presence of S-adenosyl-L-methionine, whereas N3-methylcytosine32 does not form in tRNASer1 in vitro, indicating the absence of a factor(s) required for tRNASer1 N3-methylcytosine32 formation
-
-
?
S-adenosyl-L-methionine + cytosine32 in tRNA1Thr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Thr
tRNAThr1 = tRNAThr(IGU). Because position 32 of tRNA has an important role in accurate codon recognition, N3-methylcytosine32 formation in tRNAThr1 or tRNASer1 might play a role in modulating codon recognition and translational efficiency
-
-
?
S-adenosyl-L-methionine + cytosine32 in tRNA1Thr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Thr
tRNAThr1 = tRNAThr(IGU). ABP140 is identified as the protein responsible for N3-methylcytosine32 formation in both tRNAThr1 and tRNASer1 by systematic reverse genetic approach combined with mass spectrometry (ribonucleome analysis). N3-Methylcytosine32 formation in tRNAThr1 can be reconstituted using recombinant Abp140p in the presence of S-adenosyl-L-methionine, whereas N3-methylcytosine32 does not form in tRNASer1 in vitro, indicating the absence of a factor(s) required for tRNASer1 N3-methylcytosine32 formation
-
-
?
S-adenosyl-L-methionine + cytosine32 in tRNA1Thr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Thr
tRNAThr1 = tRNAThr(IGU). Trm140p does not have detectable activity on a tRNAThr(IGU) transcript with a C32A mutation. No activity with tRNAPhe. It is demonstrated directly that ABP140 is required for the m3C modification of tRNAThr(IGU) in yeast, and it is infered that ABP140 is required for m3C32 formation for all six tRNAThr and tRNASer species for which m3C is documented
-
-
?
S-adenosyl-L-methionine + cytosine32 in tRNASer
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNASer
-
-
-
?
S-adenosyl-L-methionine + cytosine32 in tRNASer
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNASer
best tRNASer substrate is tRNASer(UGA), lower activity with tRNASer(GCU) and tRNASer(CGA)
-
-
?
S-adenosyl-L-methionine + cytosine32 in tRNASer
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNASer
-
-
-
?
S-adenosyl-L-methionine + cytosine32 in tRNASer
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNASer
best tRNASer substrate is tRNASer(UGA), lower activity with tRNASer(GCU) and tRNASer(CGA)
-
-
?
S-adenosyl-L-methionine + cytosine32 in tRNAThr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr
-
-
-
?
S-adenosyl-L-methionine + cytosine32 in tRNAThr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr
-
-
-
?
additional information
?
-
Trm140 interacts with Ses1, a cytoplasmic serine-tRNA ligase (EC 6.1.1.11). Ses1 stimulates m3C formation of tRNASer species
-
-
-
additional information
?
-
substrate specificity of enzyme Trm140 in vitro and in vivo, overview. An XGU anticodon and t6A37 are necessary and sufficient for m3C modification of tRNAThr species. tRNAThr(CGU) scaffold used for analysis of tRNAThr variants is fully functional and efficiently modified to m3C. For the tRNAThr(CGU) 28,50 variants, substitution of G35 or U36 with each of the other three nucleotides almost completely abolishes the copurification of tRNA, whereas substitution of C34 with other nucleotides leads to high levels of variant copurification. Trm140 binds tRNAs with a G35-U36 anticodon. G35 and U36 of tRNAThr(CGU) are required for m3C formation. Trm140 specifically binds tRNAThr substrates, activities with tRNAThr variants, overview
-
-
-
additional information
?
-
Trm140 interacts with Ses1, a cytoplasmic serine-tRNA ligase (EC 6.1.1.11). Ses1 stimulates m3C formation of tRNASer species
-
-
-
additional information
?
-
substrate specificity of enzyme Trm140 in vitro and in vivo, overview. An XGU anticodon and t6A37 are necessary and sufficient for m3C modification of tRNAThr species. tRNAThr(CGU) scaffold used for analysis of tRNAThr variants is fully functional and efficiently modified to m3C. For the tRNAThr(CGU) 28,50 variants, substitution of G35 or U36 with each of the other three nucleotides almost completely abolishes the copurification of tRNA, whereas substitution of C34 with other nucleotides leads to high levels of variant copurification. Trm140 binds tRNAs with a G35-U36 anticodon. G35 and U36 of tRNAThr(CGU) are required for m3C formation. Trm140 specifically binds tRNAThr substrates, activities with tRNAThr variants, overview
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
S-adenosyl-L-methionine + cytosine32 in tRNA1Ser
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Ser
tRNASer1 = tRNASer(UGA). Because position 32 of tRNA has an important role in accurate codon recognition, N3-methylcytosine32 formation in tRNAThr1 or tRNASer1 might play a role in modulating codon recognition and translational efficiency
-
-
?
S-adenosyl-L-methionine + cytosine32 in tRNA1Thr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Thr
tRNAThr1 = tRNAThr(IGU). Because position 32 of tRNA has an important role in accurate codon recognition, N3-methylcytosine32 formation in tRNAThr1 or tRNASer1 might play a role in modulating codon recognition and translational efficiency
-
-
?
S-adenosyl-L-methionine + cytosine32 in tRNASer
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNASer
S-adenosyl-L-methionine + cytosine32 in tRNAThr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr
additional information
?
-
S-adenosyl-L-methionine + cytosine32 in tRNASer
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNASer
-
-
-
?
S-adenosyl-L-methionine + cytosine32 in tRNASer
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNASer
-
-
-
?
S-adenosyl-L-methionine + cytosine32 in tRNAThr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr
-
-
-
?
S-adenosyl-L-methionine + cytosine32 in tRNAThr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr
-
-
-
?
additional information
?
-
Trm140 interacts with Ses1, a cytoplasmic serine-tRNA ligase (EC 6.1.1.11). Ses1 stimulates m3C formation of tRNASer species
-
-
-
additional information
?
-
Trm140 interacts with Ses1, a cytoplasmic serine-tRNA ligase (EC 6.1.1.11). Ses1 stimulates m3C formation of tRNASer species
-
-
-
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.
evolution
in the yeast Saccharomyces cerevisiae, formation of m3C32 requires Trm140 for six tRNA substrates, including three tRNAThr species and three tRNASer species, whereas in Schizosaccharomyces pombe, two Trm140 homologues are used, one for tRNAThr and one for tRNASer. The occurrence of a single Trm140 homologue is conserved broadly among Ascomycota, whereas multiple Trm140-related homologues are found in metazoans and other fungi
evolution
-
in the yeast Saccharomyces cerevisiae, formation of m3C32 requires Trm140 for six tRNA substrates, including three tRNAThr species and three tRNASer species, whereas in Schizosaccharomyces pombe, two Trm140 homologues are used, one for tRNAThr and one for tRNASer. The occurrence of a single Trm140 homologue is conserved broadly among Ascomycota, whereas multiple Trm140-related homologues are found in metazoans and other fungi
-
malfunction
knockout strains in the yeast Saccharomyces cerevisiae lack N3-methylcytosine32 in tRNA1Thr. Lack of the m3C modification does impair translation, albeit mildly
malfunction
N3-methylcytosine32 modification is absent in strains that lack the entire ABP140 gene
malfunction
specific reduction of N3-methylcytosine formation in HeLa cells by siRNA-mediated knock down of METTL2B
physiological function
N3-methylcytosine32 formation in tRNAThr1 or tRNASer1 might play a role in modulating codon recognition and translational efficiency
physiological function
the 3-methylcytidine (m3C) modification is ubiquitous in eukaryotic tRNA, widely found at C32 in the anticodon loop of tRNAThr, tRNASer, and some tRNAArg species, as well as in the variable loop (V-loop) of certain tRNASer species. In the yeast Saccharomyces cerevisiae, formation of m3C32 requires Trm140 for six tRNA substrates, including three tRNAThr species and three tRNASer species. Trm140 binding is a significant driving force for tRNA modification and suggest separate contributions from each recognition element for the modification
physiological function
-
the 3-methylcytidine (m3C) modification is ubiquitous in eukaryotic tRNA, widely found at C32 in the anticodon loop of tRNAThr, tRNASer, and some tRNAArg species, as well as in the variable loop (V-loop) of certain tRNASer species. In the yeast Saccharomyces cerevisiae, formation of m3C32 requires Trm140 for six tRNA substrates, including three tRNAThr species and three tRNASer species. Trm140 binding is a significant driving force for tRNA modification and suggest separate contributions from each recognition element for the modification
-
additional information
enzyme Trm140 has two recognition modes for 3-methylcytidine modification of the anticodon loop of tRNA substrates. Trm140 recognizes G35-U36-t6A37 of the anticodon loop of tRNAThr substrates, and this sequence is an identity element because it can be used to direct m3C modification of tRNAPhe. Trm140 recognition of tRNASer substrates is different, since their anticodons do not share G35-U36 and do not have any nucleotides in common. Rather, specificity of Trm140 for tRNASer is achieved by seryl-tRNA synthetase and the distinctive tRNASer V-loop, as well as by t6A37 and i6A37
additional information
-
enzyme Trm140 has two recognition modes for 3-methylcytidine modification of the anticodon loop of tRNA substrates. Trm140 recognizes G35-U36-t6A37 of the anticodon loop of tRNAThr substrates, and this sequence is an identity element because it can be used to direct m3C modification of tRNAPhe. Trm140 recognition of tRNASer substrates is different, since their anticodons do not share G35-U36 and do not have any nucleotides in common. Rather, specificity of Trm140 for tRNASer is achieved by seryl-tRNA synthetase and the distinctive tRNASer V-loop, as well as by t6A37 and i6A37
-
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.
D'Silva, S.; Haider, S.J.; Phizicky, E.M.
A domain of the actin binding protein Abp140 is the yeast methyltransferase responsible for 3-methylcytidine modification in the tRNA anti-codon loop
RNA
17
1100-1110
2011
Saccharomyces cerevisiae (Q08641), Saccharomyces cerevisiae
brenda
Noma, A.; Yi, S.; Katoh, T.; Takai, Y.; Suzuki, T.; Suzuki, T.
Actin-binding protein ABP140 is a methyltransferase for 3-methylcytidine at position 32 of tRNAs in Saccharomyces cerevisiae
RNA
17
1111-1119
2011
Saccharomyces cerevisiae (Q08641), Saccharomyces cerevisiae, Homo sapiens (Q6P1Q9), Homo sapiens
brenda
Han, L.; Marcus, E.; DSilva, S.; Phizicky, E.
S. cerevisiae Trm140 has two recognition modes for 3-methylcytidine modification of the anticodon loop of tRNA substrates
RNA
23
406-419
2017
Saccharomyces cerevisiae (Q08641), Saccharomyces cerevisiae ATCC 204508 (Q08641)
brenda