Elevated ATPase Activity of KaiC Applies a Circadian Checkpoint on Cell Division in Synechococcus elongatus

被引:117
作者
Dong, Guogang [1 ,2 ]
Yang, Qiong [4 ]
Wang, Qiang [3 ]
Kim, Yong-Ick [2 ]
Wood, Thammajun L. [1 ]
Osteryoung, Katherine W. [3 ]
van Oudenaarden, Alexander [4 ,5 ]
Golden, Susan S. [1 ,2 ]
机构
[1] Texas A&M Univ, Dept Biol, Ctr Biol Clocks Res, College Stn, TX 77843 USA
[2] Univ Calif San Diego, Div Biol Sci, Ctr Chronobiol, La Jolla, CA 92093 USA
[3] Michigan State Univ, Dept Plant Biol, E Lansing, MI 48824 USA
[4] MIT, Dept Phys, Cambridge, MA 02139 USA
[5] MIT, Dept Biol, Cambridge, MA 02139 USA
关键词
GENE-EXPRESSION; BACILLUS-SUBTILIS; CLOCK SYSTEM; CYANOBACTERIA; PHOSPHORYLATION; PROTEIN; IDENTIFICATION; OSCILLATION; DOMAIN; FTSZ;
D O I
10.1016/j.cell.2009.12.042
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
070307 [化学生物学]; 071010 [生物化学与分子生物学];
摘要
A circadian clock coordinates physiology and behavior in diverse groups of living organisms. Another major cyclic cellular event, the cell cycle, is regulated by the circadian clock in the few cases where linkage of these cycles has been studied. In the cyanobacterium Synechococcus elongatus, the circadian clock gates cell division by an unknown mechanism. Using timelapse microscopy, we confirm the gating of cell division in the wild-type and demonstrate the regulation of cytokinesis by key clock components. Specifically, a state of the oscillator protein KaiC that is associated with elevated ATPase activity closes the gate by acting through a known clock output pathway to inhibit FtsZ ring formation at the division site. An activity that stimulates KaiC phosphorylation independently of the KaiA protein was also uncovered. We propose a model that separates the functions of KaiC ATPase and phosphorylation in cell division gating and other circadian behaviors.
引用
收藏
页码:529 / 539
页数:11
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