Genetic and biochemical characterization of the MinC-FtsZ interaction in Bacillus subtilis.

Cell division in bacteria is regulated by proteins that interact with FtsZ and modulate its ability to polymerize into the Z ring structure. The best studied of these regulators is MinC, an inhibitor of FtsZ polymerization that plays a crucial role in the spatial control of Z ring formation. Recent...

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Autores principales:	Valdir Blasios, Alexandre W Bisson-Filho, Patricia Castellen, Maria Luiza C Nogueira, Jefferson Bettini, Rodrigo V Portugal, Ana Carolina M Zeri, Frederico J Gueiros-Filho
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/87a38febd2294850be8c9a19187f2455
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spelling	oai:doaj.org-article:87a38febd2294850be8c9a19187f24552021-11-18T07:50:25ZGenetic and biochemical characterization of the MinC-FtsZ interaction in Bacillus subtilis.1932-620310.1371/journal.pone.0060690https://doaj.org/article/87a38febd2294850be8c9a19187f24552013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23577149/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Cell division in bacteria is regulated by proteins that interact with FtsZ and modulate its ability to polymerize into the Z ring structure. The best studied of these regulators is MinC, an inhibitor of FtsZ polymerization that plays a crucial role in the spatial control of Z ring formation. Recent work established that E. coli MinC interacts with two regions of FtsZ, the bottom face of the H10 helix and the extreme C-terminal peptide (CTP). Here we determined the binding site for MinC on Bacillus subtilis FtsZ. Selection of a library of FtsZ mutants for survival in the presence of Min overexpression resulted in the isolation of 13 Min-resistant mutants. Most of the substitutions that gave rise to Min resistance clustered around the H9 and H10 helices in the C-terminal domain of FtsZ. In addition, a mutation in the CTP of B. subtilis FtsZ also produced MinC resistance. Biochemical characterization of some of the mutant proteins showed that they exhibited normal polymerization properties but reduced interaction with MinC, as expected for binding site mutations. Thus, our study shows that the overall architecture of the MinC-FtsZ interaction is conserved in E. coli and B. subtilis. Nevertheless, there was a clear difference in the mutations that conferred Min resistance, with those in B. subtilis FtsZ pointing to the side of the molecule rather than to its polymerization interface. This observation suggests that the mechanism of Z ring inhibition by MinC differs in both species.Valdir BlasiosAlexandre W Bisson-FilhoPatricia CastellenMaria Luiza C NogueiraJefferson BettiniRodrigo V PortugalAna Carolina M ZeriFrederico J Gueiros-FilhoPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 4, p e60690 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Valdir Blasios Alexandre W Bisson-Filho Patricia Castellen Maria Luiza C Nogueira Jefferson Bettini Rodrigo V Portugal Ana Carolina M Zeri Frederico J Gueiros-Filho Genetic and biochemical characterization of the MinC-FtsZ interaction in Bacillus subtilis.
description	Cell division in bacteria is regulated by proteins that interact with FtsZ and modulate its ability to polymerize into the Z ring structure. The best studied of these regulators is MinC, an inhibitor of FtsZ polymerization that plays a crucial role in the spatial control of Z ring formation. Recent work established that E. coli MinC interacts with two regions of FtsZ, the bottom face of the H10 helix and the extreme C-terminal peptide (CTP). Here we determined the binding site for MinC on Bacillus subtilis FtsZ. Selection of a library of FtsZ mutants for survival in the presence of Min overexpression resulted in the isolation of 13 Min-resistant mutants. Most of the substitutions that gave rise to Min resistance clustered around the H9 and H10 helices in the C-terminal domain of FtsZ. In addition, a mutation in the CTP of B. subtilis FtsZ also produced MinC resistance. Biochemical characterization of some of the mutant proteins showed that they exhibited normal polymerization properties but reduced interaction with MinC, as expected for binding site mutations. Thus, our study shows that the overall architecture of the MinC-FtsZ interaction is conserved in E. coli and B. subtilis. Nevertheless, there was a clear difference in the mutations that conferred Min resistance, with those in B. subtilis FtsZ pointing to the side of the molecule rather than to its polymerization interface. This observation suggests that the mechanism of Z ring inhibition by MinC differs in both species.
format	article
author	Valdir Blasios Alexandre W Bisson-Filho Patricia Castellen Maria Luiza C Nogueira Jefferson Bettini Rodrigo V Portugal Ana Carolina M Zeri Frederico J Gueiros-Filho
author_facet	Valdir Blasios Alexandre W Bisson-Filho Patricia Castellen Maria Luiza C Nogueira Jefferson Bettini Rodrigo V Portugal Ana Carolina M Zeri Frederico J Gueiros-Filho
author_sort	Valdir Blasios
title	Genetic and biochemical characterization of the MinC-FtsZ interaction in Bacillus subtilis.
title_short	Genetic and biochemical characterization of the MinC-FtsZ interaction in Bacillus subtilis.
title_full	Genetic and biochemical characterization of the MinC-FtsZ interaction in Bacillus subtilis.
title_fullStr	Genetic and biochemical characterization of the MinC-FtsZ interaction in Bacillus subtilis.
title_full_unstemmed	Genetic and biochemical characterization of the MinC-FtsZ interaction in Bacillus subtilis.
title_sort	genetic and biochemical characterization of the minc-ftsz interaction in bacillus subtilis.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/87a38febd2294850be8c9a19187f2455
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Genetic and biochemical characterization of the MinC-FtsZ interaction in Bacillus subtilis.

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