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