Journal
ANNUAL REVIEW OF BIOPHYSICS, VOL 40
Volume 40, Issue -, Pages 99-117Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev-biophys-042910-155329
Keywords
chromatin; nucleosome assembly and disassembly; single-molecule approaches; histone chaperone; kinetics; thermodynamics
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Funding
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM082837, F32GM083532] Funding Source: NIH RePORTER
- Howard Hughes Medical Institute Funding Source: Medline
- NIGMS NIH HHS [F32 GM083532, R01GM082837, F32GM083532] Funding Source: Medline
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Chromatin is a highly regulated, modular nucleoprotein complex that is central to many processes in eukaryotes. The organization of DNA into nucleosomes and higher-order structures has profound implications for DNA accessibility. Alternative structural states of the nucleosome, and the thermodynamic parameters governing its assembly and disassembly, need to be considered in order to understand how access to nucleosomal DNA is regulated. In this review, we provide a brief historical account of how the overriding perception regarding aspects of nucleosome structure has changed over the past thirty years. We discuss recent technical advances regarding nucleosome structure and its physical characterization and review the evidence for alternative nucleosome conformations and their implications for nucleosome and chromatin dynamics.
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