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  1. B200 工学部/工学研究科
  2. B200a 雑誌掲載論文
  3. 学術雑誌

Effects of Stochastic Single-Molecule Reactions on Coherent Ensemble Oscillations in the KaiABC Circadian Clock

http://hdl.handle.net/2237/00030140
617146cf-0e36-4bea-866f-985aab532cc0
名前 / ファイル ライセンス アクション
JPCB_Sasai_rev_for_PDF.pdf JPCB_Sasai_rev_for_PDF (1.7 MB)
Item type 学術雑誌論文 / Journal Article(1)
公開日 2019-05-09
タイトル
タイトル Effects of Stochastic Single-Molecule Reactions on Coherent Ensemble Oscillations in the KaiABC Circadian Clock
著者 Sasai, Masaki

× Sasai, Masaki

WEKO 90969

Sasai, Masaki

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権利
権利情報 “This document is the Accepted Manuscript version of a Published Work that appeared in final form in [The Journal of Physical Chemistry B], copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see [https://pubs.acs.org/articlesonrequest/AOR-idnsys9JeWi7JiTBrq25].”
抄録
内容記述 How do many constituent molecules in a biochemical system synchronize, giving rise to coherent system-level oscillations? One system that is particularly suitable for use in studying this problem is a mixture solution of three cyanobacterial proteins, KaiA, KaiB, and KaiC: the phosphorylation level of KaiC shows stable oscillations with a period of approximately 24 h when these three Kai proteins are incubated with ATP in vitro. Here, we analyze the mechanism behind synchronization in the KaiABC system theoretically by enhancing a model previously developed by the present author. Our simulation results suggest that positive feedback between stochastic ATP hydrolysis and the allosteric structural transitions in KaiC molecules drives oscillations of individual molecules and promotes synchronization of oscillations of many KaiC molecules. Our simulations also show that the ATPase activity of KaiC is correlated with the oscillation frequency of an ensemble of KaiC molecules. These results suggest that stochastic ATP hydrolysis in each KaiC molecule plays an important role in regulating the coherent system-level oscillations. This property is robust against changes in the binding and unbinding rate constants for KaiA to/from KaiC or KaiB, but the oscillations are sensitive to the rate constants of the KaiC phosphorylation and dephosphorylation reactions.
内容記述タイプ Abstract
内容記述
内容記述 ファイル公開:2020-01-24
内容記述タイプ Other
出版者
出版者 ACS Publications
言語
言語 eng
資源タイプ
資源タイプresource http://purl.org/coar/resource_type/c_6501
タイプ journal article
DOI
関連識別子
識別子タイプ DOI
関連識別子 https://doi.org/10.1021/acs.jpcb.8b10584
ISSN(print)
収録物識別子タイプ ISSN
収録物識別子 1520-6106
書誌情報 The Journal of Physical Chemistry B

巻 123, 号 3, p. 702-713, 発行日 2019-01-24
著者版フラグ
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