The influence of KaiA mutations on its function in the KaiABC circadian clock system

The core oscillator of the circadian clock of cyanobacteria consists of three proteins, KaiA, KaiB, and KaiC. The KaiABC oscillator can be re-constituted in vitro with the purified proteins in buffer containing ATP and Mg(2+). The interaction between KaiA and KaiC has not been well studied. In this...

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Detalles Bibliográficos
Autores principales: Chen, Qiang, Liu, Sen, Yang, Liting, Zhang, Lingya, Li, Jinkui
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2018
Materias:
Proteomics and Biochemistry   
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5996256/
https://www.ncbi.nlm.nih.gov/pubmed/29900192
http://dx.doi.org/10.1016/j.dib.2018.03.032
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author Chen, Qiang
Liu, Sen
Yang, Liting
Zhang, Lingya
Li, Jinkui
author_facet Chen, Qiang
Liu, Sen
Yang, Liting
Zhang, Lingya
Li, Jinkui
author_sort Chen, Qiang
collection PubMed
description The core oscillator of the circadian clock of cyanobacteria consists of three proteins, KaiA, KaiB, and KaiC. The KaiABC oscillator can be re-constituted in vitro with the purified proteins in buffer containing ATP and Mg(2+). The interaction between KaiA and KaiC has not been well studied. In this article, different KaiA mutants were designed and used to elucidate the influence of KaiA structure on its function in the in vitro system. Molecular dynamics simulations were adopted to study the structural flexibility of KaiA homodimer. The data presented in this article provide further experimental supports to our work in Chen et al. (2017) [1].
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spelling pubmed-59962562018-06-13 The influence of KaiA mutations on its function in the KaiABC circadian clock system Chen, Qiang Liu, Sen Yang, Liting Zhang, Lingya Li, Jinkui Data Brief Proteomics and Biochemistry    The core oscillator of the circadian clock of cyanobacteria consists of three proteins, KaiA, KaiB, and KaiC. The KaiABC oscillator can be re-constituted in vitro with the purified proteins in buffer containing ATP and Mg(2+). The interaction between KaiA and KaiC has not been well studied. In this article, different KaiA mutants were designed and used to elucidate the influence of KaiA structure on its function in the in vitro system. Molecular dynamics simulations were adopted to study the structural flexibility of KaiA homodimer. The data presented in this article provide further experimental supports to our work in Chen et al. (2017) [1]. Elsevier 2018-03-12 /pmc/articles/PMC5996256/ /pubmed/29900192 http://dx.doi.org/10.1016/j.dib.2018.03.032 Text en © 2018 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Proteomics and Biochemistry   
Chen, Qiang
Liu, Sen
Yang, Liting
Zhang, Lingya
Li, Jinkui
The influence of KaiA mutations on its function in the KaiABC circadian clock system
title The influence of KaiA mutations on its function in the KaiABC circadian clock system
title_full The influence of KaiA mutations on its function in the KaiABC circadian clock system
title_fullStr The influence of KaiA mutations on its function in the KaiABC circadian clock system
title_full_unstemmed The influence of KaiA mutations on its function in the KaiABC circadian clock system
title_short The influence of KaiA mutations on its function in the KaiABC circadian clock system
title_sort influence of kaia mutations on its function in the kaiabc circadian clock system
topic Proteomics and Biochemistry   
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5996256/
https://www.ncbi.nlm.nih.gov/pubmed/29900192
http://dx.doi.org/10.1016/j.dib.2018.03.032
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