Histone chaperones include a wide variety of proteins which associate with histones and regulate chromatin structure. The classic H2A–H2B type of histone chaperones, and the chromatin remodeling complex components possessing H2A–H2B chaperone activity, show a broad range of structures and functions. Rapid progress in the structural and functional study of H2A–H2B chaperones extends our knowledge about the epigenetic regulation of chromatin. In this review, we summarize the most recent advances in the understanding of the structure and function of H2A–H2B chaperones that interact with either canonical or variant H2A–H2B dimers. We discuss the current knowledge of the H2A–H2B chaperones, which present no preference for canonical and variant H2A–H2B dimers, describing how they interact with H2A–H2B to fulfill their functions. We also review recent advances of H2A variant-specific chaperones, demarcating how they achieve specific recognition for histone variant H2A.Z and how these interactions regulate chromatin structure by nucleosome editing. We highlight the universal mechanism underlying H2A–H2B dimers recognition by a large variety of histone chaperones. These findings will shed insight into the biological impacts of histone chaperone, chromatin remodeling complex, and histone variants in chromatin regulation.
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September 2020
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Cover Image
Cover Image
The cover image is of a molecularly modelled receptor heterodimeric complex in its ligand bound active state (left), juxtaposed to uncomplexed receptors (right) in the presence of the proof of concept inhibitor which prevents ligand bound complex formation. For more information, see the article by Colomba and colleagues (pp. 3329–3347). The image was created by Phospho Biomedical Animation and provided by Peter Parker.
Review Article|
September 17 2020
Mechanistic and structural insights into histone H2A–H2B chaperone in chromatin regulation
Yan Huang;
Yan Huang
*
1National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China
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Yaxin Dai;
Yaxin Dai
*
1National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China
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Zheng Zhou
1National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China
2Institute of Biophysics, University of Chinese Academy of Sciences, Beijing 100049, China
Correspondence: Zheng Zhou (zhouzh@ibp.ac.cn)
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Publisher: Portland Press Ltd
Received:
April 20 2020
Revision Received:
August 15 2020
Accepted:
August 21 2020
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 2020 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society
2020
Biochem J (2020) 477 (17): 3367–3386.
Article history
Received:
April 20 2020
Revision Received:
August 15 2020
Accepted:
August 21 2020
Citation
Yan Huang, Yaxin Dai, Zheng Zhou; Mechanistic and structural insights into histone H2A–H2B chaperone in chromatin regulation. Biochem J 18 September 2020; 477 (17): 3367–3386. doi: https://doi.org/10.1042/BCJ20190852
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