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Briefings in Functional Genomics and Proteomics Advance Access published online on May 10, 2006
Briefings in Functional Genomics and Proteomics, 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

Original Article

Histone variants--the structure behind the function

Juan Ausió *

* To whom correspondence should be addressed.
Juan Ausió, E-mail: jausio{at}uvic.ca


  Abstract

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.

Juan Ausió (PhD, University of Barcelona) has worked in the area of structural and functional characterization of histones and chromatin since 1976. He has made important contributions to the biophysical characterization of the nucleosome core particle in solution [Weizmann Institute of Science, Israel (1981-84)] and acetylated chromatin [Biochemistry and Biophysics Department, Oregon State University (1984-86)]. His current work on histone variants is carried out at the Department of Biochemistry and Microbiology at the University of Victoria where he is a Professor.


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