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PMID: 24474762 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Insight into cyanobacterial circadian timing from structural details of the KaiB-KaiC interaction.

Snijder J, Burnley RJ, Wiegard A, Melquiond AS, Bonvin AM, Axmann IM, Heck AJ

Abstract

Circadian timing in cyanobacteria is determined by the Kai system consisting of KaiA, KaiB, and KaiC. Interactions between Kai proteins change the phosphorylation status of KaiC, defining the phase of circadian timing. The KaiC-KaiB interaction is crucial for the circadian rhythm to enter the dephosphorylation phase but it is not well understood. Using mass spectrometry to characterize Kai complexes, we found that KaiB forms monomers, dimers, and tetramers. The monomer is the unit that interacts with KaiC, with six KaiB monomers binding to one KaiC hexamer. Hydrogen-deuterium exchange MS reveals structural changes in KaiC upon binding of KaiB in both the CI and CII domains, showing allosteric coupling upon KaiB binding. Based on this information we propose a model of the KaiB-KaiC complex and hypothesize that the allosteric changes observed upon complex formation relate to coupling KaiC ATPase activity with KaiB binding and to sequestration of KaiA dimers into KaiCBA complexes.

Keywords
ion mobility spectrometry native MS protein–protein docking
MeSH Terms
Bacterial Proteins/metabolism Circadian Rhythm Circadian Rhythm Signaling Peptides and Proteins/metabolism Cyanobacteria/physiology Mass Spectrometry Phosphorylation Protein Binding Protein Conformation
Chemicals
Bacterial Proteins Circadian Rhythm Signaling Peptides and Proteins KaiB protein, cyanobacteria KaiC protein, cyanobacteria
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Snijder Joost
Biomolecular Mass Spectrometry and Proteomics Group, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands.
Burnley Rebecca J
Wiegard Anika
Melquiond Adrien S J
Bonvin Alexandre M J J
Axmann Ilka M
Heck Albert J R
Conflict of Interest

The authors declare no conflict of interest.

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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
1091-6490
Published
2014-01-28
Epub
2014-00-13
Pages
1379-84
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC3910634
Subset
IM
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