Scovell WM. High mobility group protein 1: A collaborator in nucleosome dynamics and estrogen-responsive gene expression. World J Biol Chem 2016; 7(2): 206-222 [PMID: 27247709 DOI: 10.4331/wjbc.v7.i2.206]
Corresponding Author of This Article
William M Scovell, Emeritus Professor, Department of Chemistry, Bowling Green State University, Bowling Green, OH 43403, United States. wscovel@bgsu.edu
Research Domain of This Article
Biochemistry & Molecular Biology
Article-Type of This Article
Review
Open-Access Policy of This Article
This article is an open-access article which was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution Non Commercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial. See: http://creativecommons.org/licenses/by-nc/4.0/
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.
Open-Access: This article is an open-access article which was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution Non Commercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial. See: http://creativecommons.org/licenses/by-nc/4.0/
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
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.
