Exchange of ADP with ATP in the CII ATPase domain promotes autophosphorylation of cyanobacterial clock protein KaiC

The cyanobacterial circadian oscillator can be reconstituted in vitro. In the presence of KaiA and KaiB, the phosphorylation state of KaiC oscillates with a periodicity of ∼24 h. KaiC is a hexameric P-loop ATPase with autophosphorylation and autodephosphorylation activities. Recently, we found that...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2014-03, Vol.111 (12), p.4455-4460
Hauptverfasser:	Nishiwaki-Ohkawa, Taeko, Kitayama, Yohko, Ochiai, Erika, Kondo, Takao
Format:	Artikel
Sprache:	eng
Schlagworte:	Active sites Adenosine Diphosphate - metabolism Adenosine triphosphatase Adenosine triphosphatases Adenosine Triphosphatases - metabolism Adenosine Triphosphate - metabolism Bacterial Proteins - metabolism Biological Sciences Circadian rhythm Circadian Rhythm Signaling Peptides and Proteins - metabolism Cyanobacteria Cyanobacteria - enzymology Cyanobacteria - metabolism Hydrolysis Molecules Monomers Nucleotides Phosphorylation Physiological regulation Protein subunits Proteins Substrate Specificity
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