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Histone chaperones in nucleosome assembly and human disease

Nature Structural & Molecular Biology volume 20, pages 14–22 (2013)Cite this article

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Abstract

Nucleosome assembly following DNA replication, DNA repair and gene transcription is critical for the maintenance of genome stability and epigenetic information. Nucleosomes are assembled by replication-coupled or replication-independent pathways with the aid of histone chaperone proteins. How these different nucleosome assembly pathways are regulated remains relatively unclear. Recent studies have provided insight into the mechanisms and the roles of histone chaperones in regulating nucleosome assembly. Alterations or mutations in factors involved in nucleosome assembly have also been implicated in cancer and other human diseases. This review highlights the recent progress and outlines future challenges in the field.

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Figure 1: Histone chaperones are key regulators of replication-coupled and replication-independent nucleosome assembly.
Figure 2: H3–H4 histone chaperones bind a H3–H4 dimer or a (H3–H4)2 tetramer.

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Acknowledgements

We apologize to those whose work could not cited in this review, owing to space limitations. We thank G. Mer for use of the Rtt106–(H3–H4)2 complex structural model coordinates. This work is supported by grants to Z.Z. from the US National Institutes of Health (GM72719, GM81838, GM99722) and the National Science Foundation of China (NSFC) Collaboration grant (31210103914). Z.Z. is supported as a scholar of the Leukemia and Lymphoma Society.

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  1. Department of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, Rochester, Minnesota, USA

    Rebecca J Burgess & Zhiguo Zhang

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  1. Rebecca J Burgess
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Correspondence to Zhiguo Zhang.

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Burgess, R., Zhang, Z. Histone chaperones in nucleosome assembly and human disease. Nat Struct Mol Biol 20, 14–22 (2013). https://doi.org/10.1038/nsmb.2461

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