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

Thammajun L. Wood, Jennifer Bridwell-Rabb, Yong Ick Kim, Tiyu Gao, Yong Gang Chang, Andy LiWang, David P. Barondeau, Susan S. Golden

Research output: Contribution to journalArticleResearchpeer-review

52 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)5804-5809
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume107
Issue number13
DOIs
Publication statusPublished - 30 Mar 2010
Externally publishedYes

Keywords

  • Biological rhythms
  • DBMIB
  • Environmental signals
  • Pseudoreceiver
  • Quinone

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