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Histone chaperones: an escort network regulating histone traffic

Journal

NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 14, Issue 11, Pages 997-U1

Publisher

NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb1318

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Funding

  1. NIGMS NIH HHS [R01 GM076020-03, GM61766, R01 GM076020, R01 GM020056-33, GM20056, R01 GM061766-08, R01 GM061766, R01 GM020056] Funding Source: Medline

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In eukaryotes, DNA is organized into chromatin in a dynamic manner that enables it to be accessed for processes such as transcription and repair. Histones, the chief protein component of chromatin, must be assembled, replaced or exchanged to preserve or change this organization according to cellular needs. Histone chaperones are key actors during histone metabolism. Here we classify known histone chaperones and discuss how they build a network to escort histone proteins. Molecular interactions with histones and their potential specificity or redundancy are also discussed in light of chaperone structural properties. The multiplicity of histone chaperone partners, including histone modifiers, nucleosome remodelers and cell-cycle regulators, is relevant to their coordination with key cellular processes. Given the current interest in chromatin as a source of epigenetic marks, we address the potential contributions of histone chaperones to epigenetic memory and genome stability.

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