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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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1437-4315
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Volume 389, Issue 4

Issues

ATP-dependent chromatosome remodeling

Verena K. Maier
  • 1Adolf-Butenandt Institut, Abt. Molekularbiologie, and Münchner Zentrum für Integrierte Proteinforschung, Ludwig-Maximilian-Universität München, Schillerstrasse 44, D-80336 München, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Mariacristina Chioda
  • 2Adolf-Butenandt Institut, Abt. Molekularbiologie, and Münchner Zentrum für Integrierte Proteinforschung, Ludwig-Maximilian-Universität München, Schillerstrasse 44, D-80336 München, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Peter B. Becker
  • 3Adolf-Butenandt Institut, Abt. Molekularbiologie, and Münchner Zentrum für Integrierte Proteinforschung, Ludwig-Maximilian-Universität München, Schillerstrasse 44, D-80336 München, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2008-03-27 | DOI: https://doi.org/10.1515/BC.2008.040

Abstract

Chromatin serves to package, protect and organize the complex eukaryotic genomes to assure their stable inheritance over many cell generations. At the same time, chromatin must be dynamic to allow continued use of DNA during a cell's lifetime. One important principle that endows chromatin with flexibility involves ATP-dependent ‘remodeling’ factors, which alter DNA-histone interactions to form, disrupt or move nucleosomes. Remodeling is well documented at the nucleosomal level, but little is known about the action of remodeling factors in a more physiological chromatin environment. Recent findings suggest that some remodeling machines can reorganize even folded chromatin fibers containing the linker histone H1, extending the potential scope of remodeling reactions to the bulk of euchromatin.

Keywords: ATPase; chromatin; linker histone; nucleosome sliding

About the article

Corresponding author


Published Online: 2008-03-27

Published in Print: 2008-04-01


Citation Information: Biological Chemistry, Volume 389, Issue 4, Pages 345–352, ISSN (Online) 14374315, ISSN (Print) 14316730, DOI: https://doi.org/10.1515/BC.2008.040.

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