2020
DOI: 10.1101/2020.04.01.021055
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Sufficiency of unidirectional allostery in KaiC in generating the cyanobacterial circadian rhythm

Abstract: The clock protein of cyanobacteria KaiC forms a homohexamer with two ring-shaped domains, C1 and C2. These domains undergo several domain-specific conformational transitions and allosterically communicate to generate a circadian rhythm. Interestingly, experiments show a possibility that C2 is independent of C1. However, detailed interplay among them remains elusive. Here we propose a mathematical model, which explicitly considers the interplay. The allostery in KaiC is here modeled to be unidirectional from C2… Show more

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Cited by 2 publications
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References 41 publications
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