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The KaiA protein of the cyanobacterial circadian oscillator is modulated by a redox-active cofactor.

ABSTRACT: The circadian rhythms exhibited in the cyanobacterium Synechococcus elongatus are generated by an oscillator comprised of the proteins KaiA, KaiB, and KaiC. An external signal that commonly affects the circadian clock is light. Previously, we reported that the bacteriophytochrome-like protein CikA passes environmental signals to the oscillator by directly binding a quinone and using cellular redox state as a measure of light in this photosynthetic organism. Here, we report that KaiA also binds the quinone analog 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone (DBMIB), and the oxidized form of DBMIB, but not its reduced form, decreases the stability of KaiA in vivo, causes multimerization in vitro, and blocks KaiA stimulation of KaiC phosphorylation, which is central to circadian oscillation. Our data suggest that KaiA directly senses environmental signals as changes in redox state and modulates the circadian clock.

SUBMITTER: Wood TL 

PROVIDER: S-EPMC2851934 | biostudies-literature | 2010 Mar

REPOSITORIES: biostudies-literature

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The KaiA protein of the cyanobacterial circadian oscillator is modulated by a redox-active cofactor.

Wood Thammajun L TL   Bridwell-Rabb Jennifer J   Kim Yong-Ick YI   Gao Tiyu T   Chang Yong-Gang YG   LiWang Andy A   Barondeau David P DP   Golden Susan S SS  

Proceedings of the National Academy of Sciences of the United States of America 20100315 13

The circadian rhythms exhibited in the cyanobacterium Synechococcus elongatus are generated by an oscillator comprised of the proteins KaiA, KaiB, and KaiC. An external signal that commonly affects the circadian clock is light. Previously, we reported that the bacteriophytochrome-like protein CikA passes environmental signals to the oscillator by directly binding a quinone and using cellular redox state as a measure of light in this photosynthetic organism. Here, we report that KaiA also binds t  ...[more]

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