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Literature summary for 2.1.1.268 extracted from

  • 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 (2011), RNA, 17, 1111-1119.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of hexahistidine-tagged Abp140p in Saccharomces cerevisiae Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
D466A no formation of N3-methylcytosine32 Saccharomyces cerevisiae
D547A decreased activity Saccharomyces cerevisiae
delD602-Q621 no formation of N3-methylcytosine32 Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
actin filament subcellular localization of ABP140 to actin filaments is not involved in tRNA modification Saccharomyces cerevisiae 5884
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
71486
-
2 * 71486, the homodimer is formed through covalent linkage(s) other than disulfide bond, calculated from sequence, SDS-PAGE Saccharomyces cerevisiae
71500
-
2 * 71500, the homodimer is formed through covalent linkage(s) other than disulfide bond, SDS-PAGE Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + cytosine32 in tRNA1Ser Saccharomyces cerevisiae 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-homocysteine + N3-methylcytosine32 in tRNA1Ser
-
?
S-adenosyl-L-methionine + cytosine32 in tRNA1Thr Saccharomyces cerevisiae 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-homocysteine + N3-methylcytosine32 in tRNA1Thr
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q6P1Q9
-
-
Saccharomyces cerevisiae Q08641
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Saccharomyces cerevisiae

Reaction

Reaction Comment Organism Reaction ID
S-adenosyl-L-methionine + cytosine32 in tRNASer = S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNASer (2) Saccharomyces cerevisiae
S-adenosyl-L-methionine + cytosine32 in tRNAThr = S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr (1) Saccharomyces cerevisiae

Source Tissue

Source Tissue Comment Organism Textmining
HeLa cell
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + cytosine32 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 Saccharomyces cerevisiae S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Ser
-
?
S-adenosyl-L-methionine + cytosine32 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 Saccharomyces cerevisiae S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Ser
-
?
S-adenosyl-L-methionine + cytosine32 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 Saccharomyces cerevisiae S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Thr
-
?
S-adenosyl-L-methionine + cytosine32 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 Saccharomyces cerevisiae S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Thr
-
?

Subunits

Subunits Comment Organism
dimer 2 * 71486, the homodimer is formed through covalent linkage(s) other than disulfide bond, calculated from sequence, SDS-PAGE Saccharomyces cerevisiae
dimer 2 * 71500, the homodimer is formed through covalent linkage(s) other than disulfide bond, SDS-PAGE Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
ABP140
-
Saccharomyces cerevisiae
METTL2B
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Saccharomyces cerevisiae

General Information

General Information Comment Organism
malfunction N3-methylcytosine32 modification is absent in strains that lack the entire ABP140 gene Saccharomyces cerevisiae
malfunction specific reduction of N3-methylcytosine formation in HeLa cells by siRNA-mediated knock down of METTL2B Homo sapiens
physiological function N3-methylcytosine32 formation in tRNAThr1 or tRNASer1 might play a role in modulating codon recognition and translational efficiency Saccharomyces cerevisiae