+検索条件
-Structure paper
タイトル | Cryo-EM structures of human mA writer complexes. |
---|---|
ジャーナル・号・ページ | Cell Res, Vol. 32, Issue 11, Page 982-994, Year 2022 |
掲載日 | 2022年9月27日 |
著者 | Shichen Su / Shanshan Li / Ting Deng / Minsong Gao / Yue Yin / Baixing Wu / Chao Peng / Jianzhao Liu / Jinbiao Ma / Kaiming Zhang / |
PubMed 要旨 | N-methyladenosine (mA) is the most abundant ribonucleotide modification among eukaryotic messenger RNAs. The mA "writer" consists of the catalytic subunit mA-METTL complex (MAC) and the regulatory ...N-methyladenosine (mA) is the most abundant ribonucleotide modification among eukaryotic messenger RNAs. The mA "writer" consists of the catalytic subunit mA-METTL complex (MAC) and the regulatory subunit mA-METTL-associated complex (MACOM), the latter being essential for enzymatic activity. Here, we report the cryo-electron microscopy (cryo-EM) structures of MACOM at a 3.0-Å resolution, uncovering that WTAP and VIRMA form the core structure of MACOM and that ZC3H13 stretches the conformation by binding VIRMA. Furthermore, the 4.4-Å resolution cryo-EM map of the MACOM-MAC complex, combined with crosslinking mass spectrometry and GST pull-down analysis, elucidates a plausible model of the mA writer complex, in which MACOM binds to MAC mainly through WTAP and METTL3 interactions. In combination with in vitro RNA substrate binding and mA methyltransferase activity assays, our results illustrate the molecular basis of how MACOM assembles and interacts with MAC to form an active mA writer complex. |
リンク | Cell Res / PubMed:36167981 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.0 - 4.4 Å |
構造データ | EMDB-31946, PDB-7vf2: EMDB-31947, PDB-7vf5: EMDB-34169: Human m6A writer complex (WTAP, VIRMA, ZC3H13, and HAKAI, METTL3, METTL14) |
由来 |
|
キーワード | RNA BINDING PROTEIN / m6A-METTL associated complex / cryo-EM / WTAP / Virma. |