Cap-specific terminal N 6-methylation of RNA by an RNA polymerase II-associated methyltransferase - PubMed (original) (raw)

. 2019 Jan 11;363(6423):eaav0080.

doi: 10.1126/science.aav0080. Epub 2018 Nov 22.

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Cap-specific terminal N 6-methylation of RNA by an RNA polymerase II-associated methyltransferase

Shinichiro Akichika et al. Science. 2019.

Abstract

N 6-methyladenosine (m6A), a major modification of messenger RNAs (mRNAs), plays critical roles in RNA metabolism and function. In addition to the internal m6A, N 6, 2'-_O_-dimethyladenosine (m6Am) is present at the transcription start nucleotide of capped mRNAs in vertebrates. However, its biogenesis and functional role remain elusive. Using a reverse genetics approach, we identified PCIF1, a factor that interacts with the serine-5-phosphorylated carboxyl-terminal domain of RNA polymerase II, as a cap-specific adenosine methyltransferase (CAPAM) responsible for N 6-methylation of m6Am. The crystal structure of CAPAM in complex with substrates revealed the molecular basis of cap-specific m6A formation. A transcriptome-wide analysis revealed that N 6-methylation of m6Am promotes the translation of capped mRNAs. Thus, a cap-specific m6A writer promotes translation of mRNAs starting from m6Am.

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