Atomic-scale origins of slowness in the cyanobacterial circadian clock

Circadian clocks generate slow and ordered cellular dynamics but consist of fast-moving bio-macromolecules; consequently, the origins of the overall slowness remain unclear. We identified the adenosine triphosphate (ATP) catalytic region [adenosine triphosphatase (ATPase)] in the amino-terminal half...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2015-07, Vol.349 (6245), p.312-316
Main Authors: Abe, Jun, Hiyama, Takuya B., Mukaiyama, Atsushi, Son, Seyoung, Mori, Toshifumi, Saito, Shinji, Osako, Masato, Wolanin, Julie, Yamashita, Eiki, Kondo, Takao, Akiyama, Shuji
Format: Article
Language:English
Subjects:
Adenosine triphosphate
Adenosines
Algae
Biochemistry
Biological clocks
Circadian rhythm
Clocks
Cyanobacteria
Kinetics
Origins
Peptides
Proteins
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Summary:Circadian clocks generate slow and ordered cellular dynamics but consist of fast-moving bio-macromolecules; consequently, the origins of the overall slowness remain unclear. We identified the adenosine triphosphate (ATP) catalytic region [adenosine triphosphatase (ATPase)] in the amino-terminal half of the clock protein KaiC as the minimal pacemaker that controls the in vivo frequency of the cyanobacterial clock. Crystal structures of the ATPase revealed that the slowness of this ATPase arises from sequestration of a lytic water molecule in an unfavorable position and coupling of ATP hydrolysis to a peptide isomerization with high activation energy. The slow ATPase is coupled with another ATPase catalyzing autodephosphorylation in the carboxyl-terminal half of KaiC, yielding the circadian response frequency of intermolecular interactions with other clock-related proteins that influences the transcription and translation cycle.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1261040