A METTL3-METTL14 complex mediates mammalian nuclear RNA N6-adenosine methylation

Nat Chem Biol. 2014 Feb;10(2):93-5. doi: 10.1038/nchembio.1432. Epub 2013 Dec 6.

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.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Adenosine / metabolism*
  • Animals
  • Base Sequence
  • Binding Sites
  • Cell Nucleus / metabolism
  • Enzyme Stability
  • HeLa Cells
  • Humans
  • Methylation
  • Methyltransferases / chemistry
  • Methyltransferases / metabolism*
  • Models, Molecular
  • Multienzyme Complexes / chemistry
  • Multienzyme Complexes / metabolism*
  • RNA / metabolism*

Substances

  • Multienzyme Complexes
  • RNA
  • METTL14 protein, human
  • Methyltransferases
  • METTL3 protein, human
  • Adenosine

Associated data

  • GEO/GSE46705
  • PubChem-Substance/170464620
  • PubChem-Substance/170464621