ATP hydrolysis by KaiC promotes its KaiA binding in the cyanobacterial circadian clock system
Abstract
The cyanobacterial clock is controlled via the interplay among KaiA, KaiB, and KaiC, which generate a periodic oscillation of KaiC phosphorylation in the presence of ATP. KaiC forms a homohexamer harboring 12 ATP-binding sites and exerts ATPase activities associated with its autophosphorylation and dephosphorylation. The KaiC nucleotide state is a determining factor of the KaiB-KaiC interaction; however, its relationship with the KaiA-KaiC...
Paper Details
Title
ATP hydrolysis by KaiC promotes its KaiA binding in the cyanobacterial circadian clock system
Published Date
Jun 1, 2019
Journal
Volume
2
Issue
3
Pages
e201900368 - e201900368
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