Skip Navigation


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
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow All Versions of this Article:
5/3/228    most recent
ell020v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Ausió, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ausió, J.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 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


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Learn. Mem.Home page
R. M. Barrett and M. A. Wood
Beyond transcription factors: The role of chromatin modifying enzymes in regulating transcription required for memory
Learn. Mem., June 26, 2008; 15(7): 460 - 467.
[Abstract] [Full Text] [PDF]

Home page
 RNAHome page
M. Davila Lopez and T. Samuelsson
Early evolution of histone mRNA 3' end processing
RNA, January 1, 2008; 14(1): 1 - 10.
[Abstract] [Full Text] [PDF]

Home page
 FASEB J.Home page
J. M. Eirin-Lopez, T. Ishibashi, and J. Ausio
H2A.Bbd: a quickly evolving hypervariable mammalian histone that destabilizes nucleosomes in an acetylation-independent way
FASEB J, January 1, 2008; 22(1): 316 - 326.
[Abstract] [Full Text] [PDF]

Home page
 FASEB J.Home page
J. Zlatanova, C. Seebart, and M. Tomschik
Nap1: taking a closer look at a juggler protein of extraordinary skills
FASEB J, May 1, 2007; 21(7): 1294 - 1310.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.