title: Intricate protein-protein interactions in the cyanobacterial circadian clock.
abstract: The cyanobacterial circadian clock consists of a post-translational oscillator (PTO) and a PTO-dependent transcription-translation feedback loop (TTFL). The PTO can be reconstituted in vitro with the KaiA, KaiB, and KaiC proteins, enabling detailed biochemical and biophysical investigations. Both the CI and the CII halves of the KaiC hexamer harbor ATPases, but only the C-terminal CII ring exhibits kinase and phospho-transferase activities. KaiA stimulates the kinase and KaiB associates with KaiC during the dephosphorylation phase and sequesters KaiA. Recent research has led to conflicting models of the KaiB-KaiC interaction, precluding a clear understanding of KaiB function and KaiABC clock mechanism.
authors.affiliation: From the Department of Biochemistry and Center for Structural Biology, Vanderbilt University, School of Medicine, Nashville, Tennessee 37232-0146 martin.egli@vanderbilt.edu.
authors.forename: Martin
authors.initials: M
authors.lastname: Egli
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D057906:Circadian Clocks; D000458:Cyanobacteria / Q000378:metabolism*; D008969:Molecular Sequence Data; D010766:Phosphorylation; D011485:Protein Binding; D011487:Protein Conformation
chemical_list: D001426:Bacterial Proteins
keywords: ATPase; Circadian Rhythm; Cyanobacteria; Electron Microscopy (EM); Enzyme Structure; Hydrogen-Deuterium Exchange; Phosphorylation; Protein-Protein Interaction; Small Angle X-ray Scattering (SAXS); X-ray Crystallography