Dephosphorylation of the core clock protein KaiC in the cyanobacterial KaiABC circadian oscillator proceeds via an ATP synthase mechanism.

@article{Egli2012DephosphorylationOT,
  title={Dephosphorylation of the core clock protein KaiC in the cyanobacterial KaiABC circadian oscillator proceeds via an ATP synthase mechanism.},
  author={Martin Egli and Tetsuya Mori and Rekha Pattanayek and Yao Xu and Ximing Qin and Carl Hirschie Johnson},
  journal={Biochemistry},
  year={2012},
  volume={51 8},
  pages={1547-58}
}
The circadian clock of the cyanobacterium Synechococcus elongatus can be reconstituted in vitro from three proteins, KaiA, KaiB, and KaiC in the presence of ATP, to tick in a temperature-compensated manner. KaiC, the central cog of this oscillator, forms a homohexamer with 12 ATP molecules bound between its N- and C-terminal domains and exhibits unusual properties. Both the N-terminal (CI) and C-terminal (CII) domains harbor ATPase activity, and the subunit interfaces between CII domains are… CONTINUE READING
Recent Discussions
This paper has been referenced on Twitter 1 time over the past 90 days. VIEW TWEETS

Citations

Publications citing this paper.
Showing 1-10 of 15 extracted citations

Similar Papers

Loading similar papers…