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©The Author(s) 2016. Published by Baishideng Publishing Group Inc. All rights reserved.
World J Biol Chem. May 26, 2016; 7(2): 206-222
Published online May 26, 2016. doi: 10.4331/wjbc.v7.i2.206
High mobility group protein 1: A collaborator in nucleosome dynamics and estrogen-responsive gene expression
William M Scovell
William M Scovell, Department of Chemistry, Bowling Green State University, Bowling Green, OH 43403, United States
Author contributions: The author solely contributed to this paper.
Supported by The National Institutes of Health [GM054357-04].
Conflict-of-interest statement: There is no conflict of interest.
Correspondence to: William M Scovell, Emeritus Professor, Department of Chemistry, Bowling Green State University, Bowling Green, OH 43403, United States. wscovel@bgsu.edu
Telephone: +1-419-3722001 Fax: +1-419-3729809
Received: June 3, 2015
Peer-review started: June 4, 2015
First decision: July 6, 2015
Revised: February 19, 2016
Accepted: March 9, 2016
Article in press: March 14, 2016
Published online: May 26, 2016
Processing time: 349 Days and 0.1 Hours
Core Tip

Core tip: Response elements or target sites for transcription factors in DNA are often found veiled within a nucleosome in a chromatin milieu and in many cases are not accessible. Although the nucleosome/chromatin network is generally repressive to transcription, there are now a number of enzymatic strategies that have now been recognized that remodel the nucleosome to facilitate transcription factor access. We recently showed that estrogen receptor does not bind to a canonical nucleosome. However, we have discovered that high mobility group protein 1 (HMGB1) restructures the nucleosome in a nonenzymatic manner to facilitate strong estrogen receptor binding. This review will provide background for this work and outline our findings, characterize the HMGB1-restructured nucleosomes and propose a working model to account for the HMGB1 restructuring activity.