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Briefings in Functional Genomics and Proteomics Advance Access originally published online on May 10, 2006
Briefings in Functional Genomics and Proteomics 2006 5(3):228-243; doi:10.1093/bfgp/ell020
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© The Author 2006. Published by Oxford University Press. All rights reserved. For permissions, please email: journals.permissions@oxfordjournals.org

Special Issue Papers

Histone variants—the structure behind the function

Juan Ausió

Juan Ausió, Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC, Canada V8W 3P6. E-mail: jausio{at}uvic.ca

In recent years, the chromatin field has witnessed a renewed interest in histone variants as pertaining to their structural role, but mainly because of the functional specificity they impart to chromatin. In this review, I am going to discuss several of the most recent structural studies on core histone (H2A.Bbd, H2A.Z, H2A.X, macroH2A, H3.3, CENP-A) and linker histone variants (histone H1 microheterogeneity) focusing on their role in nucleosome stability and chromatin fibre dynamics with special emphasis on their possible functional implications. The data accumulated to date indicates that histone variability plays an important role in the histone-mediated regulation of chromatin metabolism. Understanding and deciphering the underlying structural amino acid code behind such variability remains one of the most exciting future challenges in chromatin research.

Keywords: histones, chromatin, nucleosome, stability, dynamics


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