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doi:10.1534/genetics.107.073007
A more recent version of this article appeared on September 1, 2007.
REGULAR RESEARCH PAPERS |
Shs1 plays separable roles in septin organization and cytokinesis in Saccharomyces cerevisiae
Masayuki Iwase 1, Jianying Luo 2, Erfei Bi 2 and Akio Toh-e 3*
1 University of Tokyo
2 University of Pennsylvania School of Medicine
3 The Metropolitan Institute of Medical Science
* To whom correspondence should be addressed. E-mail: toh-e{at}rinshoken.or.jp.
Submitted on March 9, 2007
Revised on May 1, 2007
Accepted on 25 June 2007
In Saccharomyces cerevisiae, five septins (Cdc3, Cdc10, Cdc11, Cdc12, and Shs1/Sep7) form the septin ring at the bud neck during vegetative growth. We show here that disruption of SHS1 caused cold-sensitive growth in the W303 background, with cells arrested in chains, indicative of a cytokinesis defect. Surprisingly, other four septins appeared to form an apparently normal septin ring in shs1
cells grown under the restrictive condition. We found that Myo1 and Iqg1, two components of the actomyosin contractile ring, and Cyk3, a component of the septum formation, were either delocalized or mislocalized in shs1 cells, suggesting that Shs1 plays supportive roles in cytokinesis. We also found that deletion of SHS1 enhanced or suppressed the septin defect in cdc10 and cdc11 cells, respectively, suggesting that Shs1 is involved in septin organization, exerting different effects on septin-ring assembly, depending on the composition of the septin subunits. Furthermore, we constructed an shs1-100c allele that lacks the coding sequence for the C-terminal 32 amino acids. This allele still displayed the genetic interactions with the septin mutants, but did not show cytokinesis defects as described above, suggesting that the roles of Shs1 in septin organization and cytokinesis are separable.
Key Words: SHS1, Saccharomyces cerevisiae, actomyosin contractile ring, cytokinesis, septin
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