Elucidation of master allostery essential for circadian clock oscillation in cyanobacteria
| Autor: | Eiki Yamashita, Atsushi Mukaiyama, Kumiko Ito-Miwa, Yoshihiko Furuike, Damien Simon, Shuji Akiyama, Dongyan Ouyang, Takao Kondo |
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| Rok vydání: | 2022 |
| Předmět: |
Cyanobacteria
Multidisciplinary biology Circadian Rhythm Signaling Peptides and Proteins Chemistry Oscillation Period (gene) Bidirectional coupling Allosteric regulation Circadian clock biology.organism_classification Circadian Rhythm Adenosine Diphosphate Bacterial Proteins Circadian Clocks KaiC Biophysics Circadian rhythm Phosphorylation |
| Zdroj: | Science Advances. 8 |
| ISSN: | 2375-2548 |
| DOI: | 10.1126/sciadv.abm8990 |
| Popis: | Spatiotemporal allostery is the source of complex but ordered biological phenomena. To identify the structural basis for allostery that drives the cyanobacterial circadian clock, we crystallized the clock protein KaiC in four distinct states, which cover a whole cycle of phosphor-transfer events at Ser 431 and Thr 432 . The minimal set of allosteric events required for oscillatory nature is a bidirectional coupling between the coil-to-helix transition of the Ser 431 -dependent phospho-switch in the C-terminal domain of KaiC and adenosine 5′-diphosphate release from its N-terminal domain during adenosine triphosphatase cycle. An engineered KaiC protein oscillator consisting of a minimal set of the identified master allosteric events exhibited a monophosphorylation cycle of Ser 431 with a temperature-compensated circadian period, providing design principles for simple posttranslational biochemical circadian oscillators. |
| Databáze: | OpenAIRE |
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