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.
Jianzhao Liu  1 ,  Yanan Yue  1 ,  Dali Han  2 ,  Xiao Wang  2 ,  Ye Fu  2 ,  Liang Zhang  2 ,  Guifang Jia  2 ,  Miao Yu  2 ,  Zhike Lu  2 ,  Xin Deng  2 ,  Qing Dai  2 ,  Weizhong Chen  2 ,  Chuan He  2
Affiliations
  • 1. 1] Department of Chemistry, University of Chicago, Chicago, Illinois, USA. [2] Institute for Biophysical Dynamics, University of Chicago, Chicago, Illinois, USA. [3].
  • 2. 1] Department of Chemistry, University of Chicago, Chicago, Illinois, USA. [2] Institute for Biophysical Dynamics, University of Chicago, Chicago, Illinois, USA.
PMID: 24316715 DOI: 10.1038/nchembio.1432
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.