A METTL3-METTL14 complex mediates mammalian nuclear RNA N6-adenosine methylation.
Nat Chem Biol, 2014/2;10(2):93-5.
Liu J[1], Yue Y[1], Han D[2], Wang X[2], Fu Y[2], Zhang L[2], Jia G[2], Yu M[2], Lu Z[2], Deng X[2], Dai Q[2], Chen W[2], He C[2]
Affiliations
PMID: 24316715DOI: 10.1038/nchembio.1432
Impact factor: 16.174
Abstract
N(6)-methyladenosine (m(6)A) is the most prevalent and reversible internal modification in mammalian messenger and noncoding RNAs. We report here that human methyltransferase-like 14 (METTL14) catalyzes m(6)A RNA methylation. Together with METTL3, the only previously known m(6)A methyltransferase, these two proteins form a stable heterodimer core complex of METTL3-METTL14 that functions in cellular m(6)A deposition on mammalian nuclear RNAs. WTAP, a mammalian splicing factor, can interact with this complex and affect this methylation.
MeSH terms
Adenosine; Animals; Base Sequence; Binding Sites; Cell Nucleus; Enzyme Stability; HeLa Cells; Humans; Methylation; Methyltransferases; Models, Molecular; Multienzyme Complexes; RNA
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