Structural basis for MTA1c-mediated DNA N6-adenine methylation

Jiyun Chen; Rong Hu; Ying Chen; Xiaofeng Lin; Wenwen Xiang; Hong Chen; Canglin Yao; Liang Liu

doi:10.1038/s41467-022-31060-6

Nature Communications (Jun 2022)

Structural basis for MTA1c-mediated DNA N6-adenine methylation

Jiyun Chen,
Rong Hu,
Ying Chen,
Xiaofeng Lin,
Wenwen Xiang,
Hong Chen,
Canglin Yao,
Liang Liu

Affiliations

Jiyun Chen: State Key Laboratory of Cellular Stress Biology, School of Life Sciences, Xiamen University
Rong Hu: State Key Laboratory of Cellular Stress Biology, School of Life Sciences, Xiamen University
Ying Chen: State Key Laboratory of Cellular Stress Biology, School of Life Sciences, Xiamen University
Xiaofeng Lin: State Key Laboratory of Cellular Stress Biology, School of Life Sciences, Xiamen University
Wenwen Xiang: State Key Laboratory of Cellular Stress Biology, School of Life Sciences, Xiamen University
Hong Chen: State Key Laboratory of Cellular Stress Biology, School of Life Sciences, Xiamen University
Canglin Yao: Department of Biological Sciences, University of California, San Diego
Liang Liu: State Key Laboratory of Cellular Stress Biology, School of Life Sciences, Xiamen University

DOI: https://doi.org/10.1038/s41467-022-31060-6
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 15

Abstract

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DNA N6-adenine methylation (6 mA) plays a crucial role in epigenetic regulation in eukaryotes. Here, the authors determined nine crystal structures of the ciliates 6 mA methyltransferase complexes, providing the molecular basis for understanding the functions of 6 mA.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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