Characterization of C-terminal structure of MinC and its implication in evolution of bacterial cell division

Abstract Proper cell division at the mid-site of Gram-negative bacteria reflects stringent regulation by the min system (MinC, MinD and MinE). Herein we report crystal structure of the C-terminal domain of MinC from Escherichia coli (EcMinCCTD). The MinCCTD beta helical domain is engaged in a tight...

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Autores principales:	Shaoyuan Yang, Qingya Shen, Shu Wang, Chen Song, Zhen Lei, Shengnan Han, Xiaoying Zhang, Jimin Zheng, Zongchao Jia
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/8562763f18f54172919bd36793142ebb
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spelling	oai:doaj.org-article:8562763f18f54172919bd36793142ebb2021-12-02T16:08:12ZCharacterization of C-terminal structure of MinC and its implication in evolution of bacterial cell division10.1038/s41598-017-08213-52045-2322https://doaj.org/article/8562763f18f54172919bd36793142ebb2017-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-08213-5https://doaj.org/toc/2045-2322Abstract Proper cell division at the mid-site of Gram-negative bacteria reflects stringent regulation by the min system (MinC, MinD and MinE). Herein we report crystal structure of the C-terminal domain of MinC from Escherichia coli (EcMinCCTD). The MinCCTD beta helical domain is engaged in a tight homodimer, similar to Thermotoga maritima MinCCTD (TmMinCCTD). However, both EcMinCCTD and TmMinCCTD lack an α-helix (helix3) at their C-terminal tail, in comparison to Aquifex aerolicu MinCCTD (AaMinCCTD) which forms an extra interaction interface with MinD. To understand the role of this extra binding element in MinC/MinD interactions, we fused this helix (Aahelix3) to the C-terminus of EcMinC and examined its effect on cell morphology and cell growth. Our results revealed that Aahelix3 impaired normal cell division in vivo. Furthermore, results of a co-pelleting assay and binding free energy calculation suggested that Aahelix3 plays an essential role in AaMinCD complex formation, under the circumstance of lacking MinE in A. aerolicu. Combining these results with sequence analysis of MinC and MinD in different organisms, we propose an evolutionary relationship to rationalize different mechanisms in cell division positioning in various organisms.Shaoyuan YangQingya ShenShu WangChen SongZhen LeiShengnan HanXiaoying ZhangJimin ZhengZongchao JiaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-10 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Shaoyuan Yang Qingya Shen Shu Wang Chen Song Zhen Lei Shengnan Han Xiaoying Zhang Jimin Zheng Zongchao Jia Characterization of C-terminal structure of MinC and its implication in evolution of bacterial cell division
description	Abstract Proper cell division at the mid-site of Gram-negative bacteria reflects stringent regulation by the min system (MinC, MinD and MinE). Herein we report crystal structure of the C-terminal domain of MinC from Escherichia coli (EcMinCCTD). The MinCCTD beta helical domain is engaged in a tight homodimer, similar to Thermotoga maritima MinCCTD (TmMinCCTD). However, both EcMinCCTD and TmMinCCTD lack an α-helix (helix3) at their C-terminal tail, in comparison to Aquifex aerolicu MinCCTD (AaMinCCTD) which forms an extra interaction interface with MinD. To understand the role of this extra binding element in MinC/MinD interactions, we fused this helix (Aahelix3) to the C-terminus of EcMinC and examined its effect on cell morphology and cell growth. Our results revealed that Aahelix3 impaired normal cell division in vivo. Furthermore, results of a co-pelleting assay and binding free energy calculation suggested that Aahelix3 plays an essential role in AaMinCD complex formation, under the circumstance of lacking MinE in A. aerolicu. Combining these results with sequence analysis of MinC and MinD in different organisms, we propose an evolutionary relationship to rationalize different mechanisms in cell division positioning in various organisms.
format	article
author	Shaoyuan Yang Qingya Shen Shu Wang Chen Song Zhen Lei Shengnan Han Xiaoying Zhang Jimin Zheng Zongchao Jia
author_facet	Shaoyuan Yang Qingya Shen Shu Wang Chen Song Zhen Lei Shengnan Han Xiaoying Zhang Jimin Zheng Zongchao Jia
author_sort	Shaoyuan Yang
title	Characterization of C-terminal structure of MinC and its implication in evolution of bacterial cell division
title_short	Characterization of C-terminal structure of MinC and its implication in evolution of bacterial cell division
title_full	Characterization of C-terminal structure of MinC and its implication in evolution of bacterial cell division
title_fullStr	Characterization of C-terminal structure of MinC and its implication in evolution of bacterial cell division
title_full_unstemmed	Characterization of C-terminal structure of MinC and its implication in evolution of bacterial cell division
title_sort	characterization of c-terminal structure of minc and its implication in evolution of bacterial cell division
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/8562763f18f54172919bd36793142ebb
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Characterization of C-terminal structure of MinC and its implication in evolution of bacterial cell division

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