Molecular Biology of the Cell track citations

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
 QUICK SEARCH:   [advanced]


     


Originally published as MBC in Press, 10.1091/mbc.E07-05-0504 on December 12, 2007

Vol. 19, Issue 2, 682-690, February 2008

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental Materials
Right arrow All Versions of this Article:
E07-05-0504v1
19/2/682    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 arrow reprints & permissions
Google Scholar
Right arrow Articles by Takayama, Y.
Right arrow Articles by Takahashi, K.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Takayama, Y.
Right arrow Articles by Takahashi, K.

Biphasic Incorporation of Centromeric Histone CENP-A in Fission Yeast

Yuko Takayama, Hiroshi Sato, Shigeaki Saitoh, Yuki Ogiyama, Fumie Masuda, and Kohta Takahashi

Division of Cell Biology, Institute of Life Science, Kurume University, Fukuoka 839-0864, Japan

Submitted May 29, 2007; Revised November 12, 2007; Accepted November 27, 2007
Monitoring Editor: Kerry Bloom

CENP-A is a centromere-specific histone H3 variant that is essential for kinetochore formation. Here, we report that the fission yeast Schizosaccharomyces pombe has at least two distinct CENP-A deposition phases across the cell cycle: S and G2. The S phase deposition requires Ams2 GATA factor, which promotes histone gene activation. In {Delta}ams2, CENP-A fails to retain during S, but it reaccumulates onto centromeres via the G2 deposition pathway, which is down-regulated by Hip1, a homologue of HIRA histone chaperon. Reducing the length of G2 in {Delta}ams2 results in failure of CENP-A accumulation, leading to chromosome missegregation. N-terminal green fluorescent protein-tagging reduces the centromeric association of CENP-A, causing cell death in {Delta}ams2 but not in wild-type cells, suggesting that the N-terminal tail of CENP-A may play a pivotal role in the formation of centromeric nucleosomes at G2. These observations imply that CENP-A is normally localized to centromeres in S phase in an Ams2-dependent manner and that the G2 pathway may salvage CENP-A assembly to promote genome stability. The flexibility of CENP-A incorporation during the cell cycle may account for the plasticity of kinetochore formation when the authentic centromere is damaged.


This was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E07-05-0504) on December 12, 2007.

Address correspondence to: Kohta Takahashi (takahash{at}lsi.kurume-u.ac.jp)

Abbreviations used: ChIP, chromatin immunoprecipitation.







Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Copyright © 2008 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.