Multivalent interactions drive nucleosome binding and efficient chromatin deacetylation by SIRT6

Wallace H. Liu; Jie Zheng; Jessica L. Feldman; Mark A. Klein; Vyacheslav I. Kuznetsov; Craig L. Peterson; Patrick R. Griffin; John M. Denu

doi:10.1038/s41467-020-19018-y

Nature Communications (Oct 2020)

Multivalent interactions drive nucleosome binding and efficient chromatin deacetylation by SIRT6

Wallace H. Liu,
Jie Zheng,
Jessica L. Feldman,
Mark A. Klein,
Vyacheslav I. Kuznetsov,
Craig L. Peterson,
Patrick R. Griffin,
John M. Denu

Affiliations

Wallace H. Liu: Department of Biomolecular Chemistry, University of Wisconsin-Madison
Jie Zheng: Department of Molecular Medicine, Scripps Research Florida
Jessica L. Feldman: Program in Molecular Medicine, University of Massachusetts Medical School
Mark A. Klein: Department of Biomolecular Chemistry, University of Wisconsin-Madison
Vyacheslav I. Kuznetsov: Department of Biomolecular Chemistry, University of Wisconsin-Madison
Craig L. Peterson: Program in Molecular Medicine, University of Massachusetts Medical School
Patrick R. Griffin: Department of Molecular Medicine, Scripps Research Florida
John M. Denu: Department of Biomolecular Chemistry, University of Wisconsin-Madison

DOI: https://doi.org/10.1038/s41467-020-19018-y
Journal volume & issue: Vol. 11, no. 1
pp. 1 – 13

Abstract

Read online

SIRT6 plays essential roles in metabolism, tumor suppression, and DNA repair through the deacetylation of histone substrates. Here the authors use biophysical methods to investigate the molecular basis for SIRT6 interaction with the nucleosome core particle.

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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