Cryo-EM structures of human m^(6)A writer complexes

查看全文 作　　者：Shichen [1]Su;Shanshan [2]Li;Ting [1]Deng;Minsong [3]Gao;Yue [4]Yin;Baixing [1,5]Wu;Chao [4]Peng;Jianzhao [3]Liu;Jinbiao [1]Ma;Kaiming [2]Zhang

机构地区：[1]State Key Laboratory of Genetic Engineering,Collaborative Innovation Center of Genetics and Development,Multiscale Research Institute of Complex Systems,Department of Biochemistry and Biophysics,School of Life Sciences,Fudan University,Shanghai,China;[2]MOE Key Laboratory for Cellular Dynamics and Division of Life Sciences and Medicine,University of Science and Technology of China,Hefei,Anhui,China;[3]MOE Key Laboratory of Macromolecular Synthesis and Functionalization,Department of Polymer Science and Engineering,Zhejiang University,Hangzhou,Zhejiang,China;[4]National Facility for Protein Science in Shanghai,Zhangjiang Laboratory,Shanghai Advanced Research Institute,Chinese Academy of Science,Shanghai,China;[5]Guangdong Provincial Key Laboratory of Malignant Tumor Epigenetics and Gene Regulation,Guangdong-Hong Kong Joint Laboratory for RNA Medicine,RNA Biomedical Institute,Medical Research Center,Sun Yat-Sen Memorial Hospital,Sun Yat-Sen University,Guangzhou,Guangdong,China

出　　处：《Cell Research》索引2022年第32卷第11期,共13页

基　　金：supported by the National Key R&D Program of China(2018YFC1003800 to J.M.,2017YFA0506800 to J.L.);the National Natural Science Foundation of China(31971130,31230041 to J.M.,22022702,91853110,21977087 to J.L.);the Start-up Funding by University of Science and Technology of China(KY9100000032,KJ2070000080 to K.Z.);the Fundamental Research Funds for the Central Universities(WK9100000044 to K.Z.). 摘　　要：N6-methyladenosine(m^(6)A)is the most abundant ribonucleotide modification among eukaryotic messenger RNAs.The m^(6)A“writer”consists of the catalytic subunit m^(6)A-METTL complex(MAC)and the regulatory subunit m^(6)A-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-Åresolution,uncovering that WTAP and VIRMA form the core structure of MACOM and that ZC3H13 stretches the conformation by binding VIRMA.Furthermore,the 4.4-Åresolution cryo-EM map of the MACOM–MAC complex,combined with crosslinking mass spectrometry and GST pull-down analysis,elucidates a plausible model of the m^(6)A writer complex,in which MACOM binds to MAC mainly through WTAP and METTL3 interactions.In combination with in vitro RNA substrate binding and m^(6)A methyltransferase activity assays,our results illustrate the molecular basis of how MACOM assembles and interacts with MAC to form an active m^(6)A writer complex. 关键词：COMPLEX COMPLEXES latter

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Cryo-EM structures of human m^(6)A writer complexes

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