Skip Navigation



Nucleic Acids Research Advance Access published online on April 24, 2008
Nucleic Acids Research, doi:10.1093/nar/gkn203
This Article
Right arrow Full Text Freely available
Right arrow Print PDF (8752K) Freely available
Right arrow Screen PDF (995K) Freely available
Right arrowOA All Versions of this Article:
36/10/3311    most recent
gkn203v1
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 arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Kunoh, T.
Right arrow Articles by Matsumoto, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kunoh, T.
Right arrow Articles by Matsumoto, T.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Molecular Biology

Involvement of fission yeast Clr6-HDAC in regulation of the checkpoint kinase Cds1

Tatsuki Kunoh, Toshiyuki Habu and Tomohiro Matsumoto*

Radiation Biology Center and Graduate School of Biostudies, Kyoto University, Yoshidakonoe-cho, Sakyo-ku, Kyoto, Japan 606-8501

*To whom correspondence should be addressed. Tel: +81 75 753 7552; Fax: +81 75 753 7564; Email: tmatsumo{at}house.rbc.kyoto-u.ac.jp

Received February 21, 2008. Revised April 2, 2008. Accepted April 6, 2008.

Modification of the N-terminal tail of histones is required for various nuclear processes. Here, we show that fission yeast Clr6-HDAC (histone deacetylase) regulates the checkpoint kinase Cds1 when DNA replication encounters a stressful condition. We found that the global level of acetylation of histone H4 was constant throughout the normal cell cycle, but was reduced significantly when the cell recovered from the HU-induced cell cycle arrest (or slow DNA replication). We identified the Clr6-HDAC as a component responsible for the reduction in the level of the H4 acetylation. Although DNA replication was completed, the HU-induced cell cycle arrest could not be released even after removal of HU in the clr6-1 mutant. Under this experimental condition, Cds1 kinase was maintained active and remained bound tightly to chromatin. We also demonstrated that Cds1 was active even after treatment with caffeine, an inhibitor for ATM/ATR that is an activator of Cds1. These results indicate that inactivation of Cds1 requires functional Clr6-HDAC independently of the conventional DNA replication checkpoint. When DNA replication is impeded, Clr6-HDAC activity may monitor damage on chromatin structure/environment, which is required for inactivation of Cds1.

Present address: Tatsuki Kunoh, Nagahama Institute of Bio-Science and Technology, 1266 Tamura-cho, Nagahama, Shiga, Japan 526-0829


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
 Molecular Cancer TherapeuticsHome page
J. P. Alao, J. Olesch, and P. Sunnerhagen
Inhibition of type I histone deacetylase increases resistance of checkpoint-deficient cells to genotoxic agents through mitotic delay
Mol. Cancer Ther., September 1, 2009; 8(9): 2606 - 2615.
[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.