Tuning the circadian period of cyanobacteria up to 6.6 days by the single amino acid substitutions in KaiC

The circadian clock of cyanobacteria consists of only three clock proteins, KaiA, KaiB, and KaiC, which generate a circadian rhythm of KaiC phosphorylation in vitro. The adenosine triphosphatase (ATPase) activity of KaiC is the source of the 24-h period and temperature compensation. Although numerou...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2020-08, Vol.117 (34), p.20926-20931
Main Authors: Ito-Miwa, Kumiko, Furuike, Yoshihiko, Akiyama, Shuji, Kondo, Takao
Format: Article
Language:English
Subjects:
Adenosine
Adenosine triphosphatase
Adenosine Triphosphatases - metabolism
Amino Acid Substitution - genetics
Amino acids
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Biological clocks
Biological Sciences
Circadian Clocks - genetics
Circadian rhythm
Circadian Rhythm - genetics
Circadian Rhythm Signaling Peptides and Proteins - genetics
Circadian Rhythm Signaling Peptides and Proteins - metabolism
Circadian rhythms
Compensation
Cyanobacteria
Cyanobacteria - genetics
Cyanobacteria - metabolism
Gene Expression Regulation, Bacterial - genetics
Mutants
Mutation - genetics
Phosphorylation
Synechococcus - genetics
Synechococcus - metabolism
Temperature compensation
Triphosphatase
Tuning
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Summary:The circadian clock of cyanobacteria consists of only three clock proteins, KaiA, KaiB, and KaiC, which generate a circadian rhythm of KaiC phosphorylation in vitro. The adenosine triphosphatase (ATPase) activity of KaiC is the source of the 24-h period and temperature compensation. Although numerous circadian mutants of KaiC have been identified, the tuning mechanism of the 24-h period remains unclear. Here, we show that the circadian period of in vitro phosphorylation rhythm of mutants at position 402 of KaiC changed dramatically, from 15 h (0.6 d) to 158 h (6.6 d). The ATPase activities of mutants at position 402 of KaiC, without KaiA and KaiB, correlated with the frequencies (1/period), indicating that KaiC structure was the source of extra period change. Despite the wide-range tunability, temperature compensation of both the circadian period and the KaiC ATPase activity of mutants at position 402 of KaiC were nearly intact. We also found that in vivo and in vitro circadian periods and the KaiC ATPase activity of mutants at position 402 of KaiC showed a correlation with the side-chain volume of the amino acid at position 402 of KaiC. Our results indicate that residue 402 is a key position of determining the circadian period of cyanobacteria, and it is possible to dramatically alter the period of KaiC while maintaining temperature compensation.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.2005496117