Histone tail electrostatics modulate E2–E3 enzyme dynamics: a gateway to regulate ubiquitination machinery-Reference-Cited by-同舟云学术

Histone tail electrostatics modulate E2–E3 enzyme dynamics: a gateway to regulate ubiquitination machinery

Published:2023 Issue:4 Volume:25 Page:3361-3374
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Ranathunga Dineli T. S.¹^ORCID,Torabifard Hedieh¹^ORCID

Affiliation:

1. Department of Chemistry and Biochemistry, The University of Texas at Dallas, 800 West Campbell Road, Richardson, Texas 75080, USA

Abstract

Histone tail electrostatics affect conformational transitions of BRCA1/BARD1-UbcH5c (E3-E2) enzymes on the nucleosome surface that regulate H2A C-tail dynamics and ubiquitination.

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2023/CP/D2CP04059J

Reference64 articles.

1. A.Bruce , J.Alexander , L.Julian , R.Martin , R.Keith and W.Peter , Chromosomal DNA and Its Packaging in the Chromatin Fiber , NIH , 2002

2. A brief review of nucleosome structure

3. Molecular recognition of nucleosomes by binding partners

4. Chromatin Structure: A Repeating Unit of Histones and DNA

5. Crystal structure of the PRC1 ubiquitylation module bound to the nucleosome

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