Intermolecular associations determine the dynamics of the circadian KaiABC oscillator.

Abstract:

:Three proteins from cyanobacteria (KaiA, KaiB, and KaiC) can reconstitute circadian oscillations in vitro. At least three molecular properties oscillate during this reaction, namely rhythmic phosphorylation of KaiC, ATP hydrolytic activity of KaiC, and assembly/disassembly of intermolecular complexes among KaiA, KaiB, and KaiC. We found that the intermolecular associations determine key dynamic properties of this in vitro oscillator. For example, mutations within KaiB that alter the rates of binding of KaiB to KaiC also predictably modulate the period of the oscillator. Moreover, we show that KaiA can bind stably to complexes of KaiB and hyperphosphorylated KaiC. Modeling simulations indicate that the function of this binding of KaiA to the KaiB*KaiC complex is to inactivate KaiA's activity, thereby promoting the dephosphorylation phase of the reaction. Therefore, we report here dynamics of interaction of KaiA and KaiB with KaiC that determine the period and amplitude of this in vitro oscillator.

authors

Qin X,Byrne M,Mori T,Zou P,Williams DR,McHaourab H,Johnson CH

doi

10.1073/pnas.1002119107

subject

Has Abstract

pub_date

2010-08-17 00:00:00

pages

14805-10

issue

33

eissn

0027-8424

issn

1091-6490

pii

1002119107

journal_volume

107

pub_type

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