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Title

Structural insights into molecular mechanism for N6-adenosine methylation by MT-A70 family methyltransferase METTL4

Author
Publication Years
2022-09-26
DOI
Source Title
EISSN
2041-1723
Volume13Issue:1
Abstract
METTL4 belongs to a subclade of MT-A70 family members of methyltransferase (MTase) proteins shown to mediate N6-adenosine methylation for both RNA and DNA in diverse eukaryotes. Here, we report that Arabidopsis METTL4 functions as U2 snRNA MTase for N6-2'-O-dimethyladenosine (m6Am) in vivo that regulates flowering time, and specifically catalyzes N6-methylation of 2'-O-methyladenosine (Am) within a single-stranded RNA in vitro. The apo structures of full-length Arabidopsis METTL4 bound to S-adenosyl-L-methionine (SAM) and the complex structure with an Am-containing RNA substrate, combined with mutagenesis and in vitro enzymatic assays, uncover a preformed L-shaped, positively-charged cavity surrounded by four loops for substrate binding and a catalytic center composed of conserved residues for specific Am nucleotide recognition and N6-methylation activity. Structural comparison of METTL4 with the mRNA m6A enzyme METTL3/METTL14 heterodimer and modeling analysis suggest a catalytic mechanism for N6-adenosine methylation by METTL4, which may be shared among MT-A70 family members.
URL[Source Record]
Indexed By
Language
English
Important Publications
NI Journal Papers
SUSTech Authorship
Others
Funding Project
National Natural Science Foundation of China["31971130","31230041","31930017"]
WOS Research Area
Science & Technology - Other Topics
WOS Subject
Multidisciplinary Sciences
WOS Accession No
WOS:000861440000007
Publisher
Scopus EID
2-s2.0-85138634310
Data Source
Scopus
Citation statistics
Cited Times [WOS]:4
Document TypeJournal Article
Identifierhttp://kc.sustech.edu.cn/handle/2SGJ60CL/402680
DepartmentDepartment of Human Cell Biology and Genetics
南方科技大学医学院
Affiliation
1.State Key Laboratory of Genetic Engineering,Collaborative Innovation Center of Genetics and Development,Department of Biochemistry and Biophysics,Institute of Plant Biology,School of Life Sciences,Fudan University,200438,China
2.State Key Laboratory of Genetic Engineering,Collaborative Innovation Center of Genetics and Development,International Associated Laboratory of CNRS-Fudan-HUNAU on Plant Epigenome Research,Department of Biochemistry and Biophysics,Institute of Plant Biology,School of Life Sciences,Fudan University,200438,China
3.State Key Laboratory of Environmental Chemistry and Ecotoxicology,Research Center for Eco-Environmental Sciences,Chinese Academy of Sciences,University of Chinese Academy of Sciences,100085,China
4.Department of Human Cell Biology and Genetics,School of Medicine,Southern University of Science and Technology,Shenzhen,518055,China
5.Institut de Biologie Moléculaire des Plantes,CNRS,Université de Strasbourg,12 rue du Général Zimmer,67084,France
6.Ludwig Institute for Cancer Research,Oxford University,Oxford,Old Road Campus Research Building ,Roosevelt Dr ,Headington,OX3 7DQ,United Kingdom
7.Institute of Environment and Health,Jianghan University,Wuhan,430056,China
Recommended Citation
GB/T 7714
Luo,Qiang,Mo,Jiezhen,Chen,Hao,et al. Structural insights into molecular mechanism for N6-adenosine methylation by MT-A70 family methyltransferase METTL4[J]. Nature communications,2022,13(1).
APA
Luo,Qiang.,Mo,Jiezhen.,Chen,Hao.,Hu,Zetao.,Wang,Baihui.,...&Ma,Jinbiao.(2022).Structural insights into molecular mechanism for N6-adenosine methylation by MT-A70 family methyltransferase METTL4.Nature communications,13(1).
MLA
Luo,Qiang,et al."Structural insights into molecular mechanism for N6-adenosine methylation by MT-A70 family methyltransferase METTL4".Nature communications 13.1(2022).
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