Structural model of the circadian clock KaiB–KaiC complex and mechanism for modulation of KaiC phosphorylation
| Autor: | Phoebe L. Stewart, Dewight Williams, Carl Hirschie Johnson, Tetsuya Mori, Sabuj Pattanayek, Martin Egli, Rekha Pattanayek |
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| Rok vydání: | 2008 |
| Předmět: |
Models
Molecular Period (gene) Protein subunit Circadian clock macromolecular substances Random hexamer Biology Crystallography X-Ray Negative Staining Article Protein Structure Secondary General Biochemistry Genetics and Molecular Biology Protein–protein interaction Dephosphorylation Bacterial Proteins Biological Clocks KaiC KaiA Phosphorylation Protein Structure Quaternary Molecular Biology Synechococcus General Immunology and Microbiology Circadian Rhythm Signaling Peptides and Proteins General Neuroscience Cryoelectron Microscopy Peptide Fragments Circadian Rhythm Cell biology Protein Binding |
| Zdroj: | The EMBO Journal. 27:1767-1778 |
| ISSN: | 1460-2075 0261-4189 |
| DOI: | 10.1038/emboj.2008.104 |
| Popis: | The circadian clock of the cyanobacterium Synechococcus elongatus can be reconstituted in vitro by the KaiA, KaiB and KaiC proteins in the presence of ATP. The principal clock component, KaiC, undergoes regular cycles between hyper- and hypo-phosphorylated states with a period of ca. 24 h that is temperature compensated. KaiA enhances KaiC phosphorylation and this enhancement is antagonized by KaiB. Throughout the cycle Kai proteins interact in a dynamic manner to form complexes of different composition. We present a three-dimensional model of the S. elongatus KaiB-KaiC complex based on X-ray crystallography, negative-stain and cryo-electron microscopy, native gel electrophoresis and modelling techniques. We provide experimental evidence that KaiB dimers interact with KaiC from the same side as KaiA and for a conformational rearrangement of the C-terminal regions of KaiC subunits. The enlarged central channel and thus KaiC subunit separation in the C-terminal ring of the hexamer is consistent with KaiC subunit exchange during the dephosphorylation phase. The proposed binding mode of KaiB explains the observation of simultaneous binding of KaiA and KaiB to KaiC, and provides insight into the mechanism of KaiB's antagonism of KaiA. |
| Databáze: | OpenAIRE |
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