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Elucidation of master allostery essential for circadian clock oscillation in cyanobacteria
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...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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American Association for the Advancement of Science
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9012456/ https://www.ncbi.nlm.nih.gov/pubmed/35427168 http://dx.doi.org/10.1126/sciadv.abm8990 |
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author | Furuike, Yoshihiko Mukaiyama, Atsushi Ouyang, Dongyan Ito-Miwa, Kumiko Simon, Damien Yamashita, Eiki Kondo, Takao Akiyama, Shuji |
author_facet | Furuike, Yoshihiko Mukaiyama, Atsushi Ouyang, Dongyan Ito-Miwa, Kumiko Simon, Damien Yamashita, Eiki Kondo, Takao Akiyama, Shuji |
author_sort | Furuike, Yoshihiko |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-9012456 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | American Association for the Advancement of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-90124562022-04-26 Elucidation of master allostery essential for circadian clock oscillation in cyanobacteria Furuike, Yoshihiko Mukaiyama, Atsushi Ouyang, Dongyan Ito-Miwa, Kumiko Simon, Damien Yamashita, Eiki Kondo, Takao Akiyama, Shuji Sci Adv Biomedicine and Life Sciences 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. American Association for the Advancement of Science 2022-04-15 /pmc/articles/PMC9012456/ /pubmed/35427168 http://dx.doi.org/10.1126/sciadv.abm8990 Text en Copyright © 2022 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC). https://creativecommons.org/licenses/by-nc/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial license (https://creativecommons.org/licenses/by-nc/4.0/) , which permits use, distribution, and reproduction in any medium, so long as the resultant use is not for commercial advantage and provided the original work is properly cited. |
spellingShingle | Biomedicine and Life Sciences Furuike, Yoshihiko Mukaiyama, Atsushi Ouyang, Dongyan Ito-Miwa, Kumiko Simon, Damien Yamashita, Eiki Kondo, Takao Akiyama, Shuji Elucidation of master allostery essential for circadian clock oscillation in cyanobacteria |
title | Elucidation of master allostery essential for circadian clock oscillation in cyanobacteria |
title_full | Elucidation of master allostery essential for circadian clock oscillation in cyanobacteria |
title_fullStr | Elucidation of master allostery essential for circadian clock oscillation in cyanobacteria |
title_full_unstemmed | Elucidation of master allostery essential for circadian clock oscillation in cyanobacteria |
title_short | Elucidation of master allostery essential for circadian clock oscillation in cyanobacteria |
title_sort | elucidation of master allostery essential for circadian clock oscillation in cyanobacteria |
topic | Biomedicine and Life Sciences |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9012456/ https://www.ncbi.nlm.nih.gov/pubmed/35427168 http://dx.doi.org/10.1126/sciadv.abm8990 |
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