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KaiB reduces KaiC phosphorylation in the cyanobacteria’s daily biological clock

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Abstract

A circadian rhythm in the localization of KaiB was observed in the cyanobacterium Synechococcus elongatus PCC 7942.

  • KaiB interacts with a KaiA-KaiC complex during the late subjective night.
  • The binding of KaiB to KaiC leads to a significant decrease in KaiC phosphorylation.
  • Dissociation of the clock protein complex occurs following the binding of KaiB and KaiC.
  • KaiB reduces the phosphorylation enhancement effect of KaiA in both laboratory and living systems.
  • These findings suggest a new role for KaiB in linking localization, interactions, and modifications of Kai proteins within the cyanobacterial circadian clock.

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