MCB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Other Versions of this Article:
MCB.02077-06v1
27/10/3589    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
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 Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Fink, M.
Right arrow Articles by Thoma, F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Fink, M.
Right arrow Articles by Thoma, F.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, May 2007, p. 3589-3600, Vol. 27, No. 10
0270-7306/07/$08.00+0     doi:10.1128/MCB.02077-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Contribution of the Serine 129 of Histone H2A to Chromatin Structure{triangledown}

Michel Fink, Daniela Imholz, and Fritz Thoma*

Institute of Cell Biology, ETH Zurich, 8093 Zurich, Switzerland

Received 7 November 2006/ Returned for modification 19 December 2006/ Accepted 6 March 2007

Phosphorylation of a yeast histone H2A at C-terminal serine 129 has a central role in double-strand break repair. Mimicking H2A phosphorylation by replacement of serine 129 with glutamic acid (hta1-S129E) suggested that phosphorylation destabilizes chromatin structures and thereby facilitates the access of repair proteins. Here we have tested chromatin structures in hta1-S129 mutants and in a C-terminal tail deletion strain. We show that hta1-S129E affects neither nucleosome positioning in minichromosomes and genomic loci nor supercoiling of minichromosomes. Moreover, hta1-S129E has no effect on chromatin stability measured by conventional nuclease digestion, nor does it affect DNA accessibility and repair of UV-induced DNA lesions by nucleotide excision repair and photolyase in vivo. Similarly, deletion of the C-terminal tail has no effect on nucleosome positioning and stability. These data argue against a general role for the C-terminal tail in chromatin organization and suggest that phosphorylated H2A, {gamma}-H2AX in higher eukaryotes, acts by recruitment of repair components rather than by destabilizing chromatin structures.

* Corresponding author. Mailing address: Institute of Cell Biology, ETH Zurich, Schafmattstrasse 18, 8093 Zurich, Switzerland. Phone: 41 44 633 33 23. Fax: 41 44 633 10 69. E-mail: fritz.thoma{at}cell.biol.ethz.ch

{triangledown} Published ahead of print on 12 March 2007.

Molecular and Cellular Biology, May 2007, p. 3589-3600, Vol. 27, No. 10
0270-7306/07/$08.00+0     doi:10.1128/MCB.02077-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.





Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. J. Virol. Eukaryot. Cell
Microbiol. Mol. Biol. Rev. Clin. Vaccine Immunol. All ASM Journals

Copyright © 2007 by the American Society for Microbiology. All rights reserved.