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Polyamines Disrupt the KaiABC Oscillator by Inducing Protein Denaturation

Polyamines are positively charged small molecules ubiquitously existing in all living organisms, and they are considered as one kind of the most ancient cellular components. The most common polyamines are spermidine, spermine, and their precursor putrescine generated from ornithine. Polyamines play...

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Autores principales: Li, Jinkui, Zhang, Lingya, Xiong, Junwen, Cheng, Xiyao, Huang, Yongqi, Su, Zhengding, Yi, Ming, Liu, Sen
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6767301/
https://www.ncbi.nlm.nih.gov/pubmed/31540079
http://dx.doi.org/10.3390/molecules24183351
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author Li, Jinkui
Zhang, Lingya
Xiong, Junwen
Cheng, Xiyao
Huang, Yongqi
Su, Zhengding
Yi, Ming
Liu, Sen
author_facet Li, Jinkui
Zhang, Lingya
Xiong, Junwen
Cheng, Xiyao
Huang, Yongqi
Su, Zhengding
Yi, Ming
Liu, Sen
author_sort Li, Jinkui
collection PubMed
description Polyamines are positively charged small molecules ubiquitously existing in all living organisms, and they are considered as one kind of the most ancient cellular components. The most common polyamines are spermidine, spermine, and their precursor putrescine generated from ornithine. Polyamines play critical roles in cells by stabilizing chromatin structure, regulating DNA replication, modulating gene expression, etc., and they also affect the structure and function of proteins. A few studies have investigated the impact of polyamines on protein structure and function previously, but no reports have focused on a protein-based biological module with a dedicated function. In this report, we investigated the impact of polyamines (putrescine, spermidine, and spermine) on the cyanobacterial KaiABC circadian oscillator. Using an established in vitro reconstitution system, we noticed that polyamines could disrupt the robustness of the KaiABC oscillator by inducing the denaturation of the Kai proteins (KaiA, KaiB, and KaiC). Further experiments showed that the denaturation was likely due to the induced change of the thermal stability of the clock proteins. Our study revealed an intriguing role of polyamines as a component in complex cellular environments and would be of great importance for elucidating the biological function of polyamines in future.
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spelling pubmed-67673012019-10-02 Polyamines Disrupt the KaiABC Oscillator by Inducing Protein Denaturation Li, Jinkui Zhang, Lingya Xiong, Junwen Cheng, Xiyao Huang, Yongqi Su, Zhengding Yi, Ming Liu, Sen Molecules Article Polyamines are positively charged small molecules ubiquitously existing in all living organisms, and they are considered as one kind of the most ancient cellular components. The most common polyamines are spermidine, spermine, and their precursor putrescine generated from ornithine. Polyamines play critical roles in cells by stabilizing chromatin structure, regulating DNA replication, modulating gene expression, etc., and they also affect the structure and function of proteins. A few studies have investigated the impact of polyamines on protein structure and function previously, but no reports have focused on a protein-based biological module with a dedicated function. In this report, we investigated the impact of polyamines (putrescine, spermidine, and spermine) on the cyanobacterial KaiABC circadian oscillator. Using an established in vitro reconstitution system, we noticed that polyamines could disrupt the robustness of the KaiABC oscillator by inducing the denaturation of the Kai proteins (KaiA, KaiB, and KaiC). Further experiments showed that the denaturation was likely due to the induced change of the thermal stability of the clock proteins. Our study revealed an intriguing role of polyamines as a component in complex cellular environments and would be of great importance for elucidating the biological function of polyamines in future. MDPI 2019-09-14 /pmc/articles/PMC6767301/ /pubmed/31540079 http://dx.doi.org/10.3390/molecules24183351 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Li, Jinkui
Zhang, Lingya
Xiong, Junwen
Cheng, Xiyao
Huang, Yongqi
Su, Zhengding
Yi, Ming
Liu, Sen
Polyamines Disrupt the KaiABC Oscillator by Inducing Protein Denaturation
title Polyamines Disrupt the KaiABC Oscillator by Inducing Protein Denaturation
title_full Polyamines Disrupt the KaiABC Oscillator by Inducing Protein Denaturation
title_fullStr Polyamines Disrupt the KaiABC Oscillator by Inducing Protein Denaturation
title_full_unstemmed Polyamines Disrupt the KaiABC Oscillator by Inducing Protein Denaturation
title_short Polyamines Disrupt the KaiABC Oscillator by Inducing Protein Denaturation
title_sort polyamines disrupt the kaiabc oscillator by inducing protein denaturation
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6767301/
https://www.ncbi.nlm.nih.gov/pubmed/31540079
http://dx.doi.org/10.3390/molecules24183351
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