Mechanism for DPY30 and ASH2L intrinsically disordered regions to modulate the MLL/SET1 activity on chromatin

Young-Tae Lee; Alex Ayoub; Sang-Ho Park; Liang Sha; Jing Xu; Fengbiao Mao; Wei Zheng; Yang Zhang; Uhn-Soo Cho; Yali Dou

doi:10.1038/s41467-021-23268-9

Nature Communications (May 2021)

Mechanism for DPY30 and ASH2L intrinsically disordered regions to modulate the MLL/SET1 activity on chromatin

Young-Tae Lee,
Alex Ayoub,
Sang-Ho Park,
Liang Sha,
Jing Xu,
Fengbiao Mao,
Wei Zheng,
Yang Zhang,
Uhn-Soo Cho,
Yali Dou

Affiliations

Young-Tae Lee: Department of Pathology, University of Michigan
Alex Ayoub: Department of Pathology, University of Michigan
Sang-Ho Park: Department of Biological Chemistry, University of Michigan
Liang Sha: Department of Medicine, Department of Biochemistry and Molecular Medicine, University of Southern California
Jing Xu: Department of Pathology, University of Michigan
Fengbiao Mao: Department of Pathology, University of Michigan
Wei Zheng: Computational Medicine and Bioinformatics, University of Michigan
Yang Zhang: Department of Biological Chemistry, University of Michigan
Uhn-Soo Cho: Department of Biological Chemistry, University of Michigan
Yali Dou: Department of Pathology, University of Michigan

DOI: https://doi.org/10.1038/s41467-021-23268-9
Journal volume & issue: Vol. 12, no. 1
pp. 1 – 13

Abstract

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Regulation of the MLL family of histone H3K4 methyltransferases on the nucleosome core particle (NCP) remains largely unknown. Here the authors show that intrinsically disordered regions of ASH2L and DPY30 restrict the rotational dynamics of MLL1 on the NCP, allowing more efficient enzyme-substrate engagement and higher H3K4 trimethylation activity.

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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