Review abstract
Nature Structural & Molecular Biology 14, 997 - 1007 (2007)
Published online: 5 November 2007 | doi:10.1038/nsmb1318
There is an Erratum (December 2007) associated with this Review.
Histone chaperones: an escort network regulating histone traffic
Leanne De Koning1,3, Armelle Corpet1,3, James E Haber2 & Geneviève Almouzni1
Abstract
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.
- Laboratory of Nuclear Dynamics and Genome Plasticity (UMR 218); Institut Curie, 26 rue d'Ulm, 75248 Paris, France.
- Department of Biology and Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts 02454, USA.
- These authors contributed equally to this work.
Correspondence to: Geneviève Almouzni1 e-mail: genevieve.almouzni@curie.fr
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