Structural highlights
Function
AB140_YEAST S-adenosyl-L-methionine-dependent methyltransferase that mediates N(3)-methylcytidine modification of residue 32 of the tRNA anticodon loop of tRNA(Thr) and tRNA(Ser) (PubMed:21518804, PubMed:21518805, PubMed:28003514). N(3)-methylcytidine methylation of tRNA(Thr) requires the N6-threonylcarbamoylation of tRNA (t6A37) by the EKC/KEOPS complex as prerequisite (PubMed:28003514). N(3)-methylcytidine methylation of tRNA(Ser) requires the formation of N(6)-dimethylallyladenosine(37) (i6A37) by MOD5 as prerequisite (PubMed:28003514). Methylation of tRNA(Ser) is also stimulated by SES1 (PubMed:28003514). Binds F-actin and shows weak F-actin cross-linking activity (PubMed:9467951).[1] [2] [3] [4]
See Also
References
- ↑ D'Silva S, Haider SJ, Phizicky EM. A domain of the actin binding protein Abp140 is the yeast methyltransferase responsible for 3-methylcytidine modification in the tRNA anti-codon loop. RNA. 2011 Jun;17(6):1100-10. PMID:21518804 doi:10.1261/rna.2652611
- ↑ 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. 2011 Jun;17(6):1111-9. PMID:21518805 doi:10.1261/rna.2653411
- ↑ Han L, Marcus E, D'Silva S, Phizicky EM. S. cerevisiae Trm140 has two recognition modes for 3-methylcytidine modification of the anticodon loop of tRNA substrates. RNA. 2017 Mar;23(3):406-419. PMID:28003514 doi:10.1261/rna.059667.116
- ↑ Asakura T, Sasaki T, Nagano F, Satoh A, Obaishi H, Nishioka H, Imamura H, Hotta K, Tanaka K, Nakanishi H, Takai Y. Isolation and characterization of a novel actin filament-binding protein from Saccharomyces cerevisiae. Oncogene. 1998 Jan 8;16(1):121-30. PMID:9467951 doi:10.1038/sj.onc.1201487
