| Structural highlights
Function
METL6_HUMAN S-adenosyl-L-methionine-dependent methyltransferase that mediates N(3)-methylcytidine modification of residue 32 of the tRNA anticodon loop of tRNA(Ser), including tRNA(Ser)(UGA) and tRNA(Ser)(GCU) (PubMed:32923617, PubMed:34268557, PubMed:34862464, PubMed:34922197). Interaction with SARS1/SerRS is required for N(3)-methylcytidine methylation (PubMed:34268557).[1] [2] [3] [4]
References
- ↑ Ignatova VV, Kaiser S, Ho JSY, Bing X, Stolz P, Tan YX, Lee CL, Gay FPH, Lastres PR, Gerlini R, Rathkolb B, Aguilar-Pimentel A, Sanz-Moreno A, Klein-Rodewald T, Calzada-Wack J, Ibragimov E, Valenta M, Lukauskas S, Pavesi A, Marschall S, Leuchtenberger S, Fuchs H, Gailus-Durner V, de Angelis MH, Bultmann S, Rando OJ, Guccione E, Kellner SM, Schneider R. METTL6 is a tRNA m(3)C methyltransferase that regulates pluripotency and tumor cell growth. Sci Adv. 2020 Aug 26;6(35):eaaz4551. PMID:32923617 doi:10.1126/sciadv.aaz4551
- ↑ Mao XL, Li ZH, Huang MH, Wang JT, Zhou JB, Li QR, Xu H, Wang XJ, Zhou XL. Mutually exclusive substrate selection strategy by human m3C RNA transferases METTL2A and METTL6. Nucleic Acids Res. 2021 Aug 20;49(14):8309-8323. PMID:34268557 doi:10.1093/nar/gkab603
- ↑ Chen R, Zhou J, Liu L, Mao XL, Zhou X, Xie W. Crystal structure of human METTL6, the m(3)C methyltransferase. Commun Biol. 2021 Dec 3;4(1):1361. PMID:34862464 doi:10.1038/s42003-021-02890-9
- ↑ Li S, Zhou H, Liao S, Wang X, Zhu Z, Zhang J, Xu C. Structural basis for METTL6-mediated m3C RNA methylation. Biochem Biophys Res Commun. 2022 Jan 22;589:159-164. PMID:34922197 doi:10.1016/j.bbrc.2021.12.013
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