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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/CAPAM_DANRE CAPAM_DANRE] Cap-specific adenosine methyltransferase that catalyzes formation of N(6),2'-O-dimethyladenosine cap (m6A(m)) by methylating the adenosine at the second transcribed position of capped mRNAs (PubMed:30467178).<ref>PMID:30467178</ref> | | [https://www.uniprot.org/uniprot/CAPAM_DANRE CAPAM_DANRE] Cap-specific adenosine methyltransferase that catalyzes formation of N(6),2'-O-dimethyladenosine cap (m6A(m)) by methylating the adenosine at the second transcribed position of capped mRNAs (PubMed:30467178).<ref>PMID:30467178</ref> |
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| == Publication Abstract from PubMed ==
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| N (6)-methyladenosine (m(6)A), a major modification of mRNAs, plays critical roles in RNA metabolism and function. In addition to the internal m(6)A, N (6), 2'-O-dimethyladenosine (m(6)Am) 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 Ser5-phosphorylated C-terminal domain of RNA polymerase II, as cap-specific adenosine methyltransferase (CAPAM) responsible for N (6)-methylation of m(6)Am. Crystal structure of CAPAM in complex with substrates revealed the molecular basis of cap-specific m(6)A formation. A transcriptome-wide analysis revealed that N (6)-methylation of m(6)Am promotes the translation of capped mRNAs. Thus, a cap-specific m(6)A writer promotes translation of mRNAs starting from m(6)Am.
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| Cap-specific terminal N (6)-methylation of RNA by an RNA polymerase II-associated methyltransferase.,Akichika S, Hirano S, Shichino Y, Suzuki T, Nishimasu H, Ishitani R, Sugita A, Hirose Y, Iwasaki S, Nureki O, Suzuki T Science. 2018 Nov 22. pii: science.aav0080. doi: 10.1126/science.aav0080. PMID:30467178<ref>PMID:30467178</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 6is0" style="background-color:#fffaf0;"></div>
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| == References == | | == References == |
| <references/> | | <references/> |
