The Min System Disassembles FtsZ Foci and Inhibits Polar Peptidoglycan Remodeling in <named-content content-type="genus-species">Bacillus subtilis</named-content>

ABSTRACT A microfluidic system coupled with fluorescence microscopy is a powerful approach for quantitative analysis of bacterial growth. Here, we measure parameters of growth and dynamic localization of the cell division initiation protein FtsZ in Bacillus subtilis. Consistent with previous reports...

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Autores principales:	Yuanchen Yu, Jinsheng Zhou, Felix Dempwolff, Joshua D. Baker, Daniel B. Kearns, Stephen C. Jacobson
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2020
Materias:	FtsZ MinD microfluidics growth cell division peptidoglycan Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/d4340419f69e4fdc9a9f3aaecf1467ea
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spelling	oai:doaj.org-article:d4340419f69e4fdc9a9f3aaecf1467ea2021-11-15T15:57:02ZThe Min System Disassembles FtsZ Foci and Inhibits Polar Peptidoglycan Remodeling in <named-content content-type="genus-species">Bacillus subtilis</named-content>10.1128/mBio.03197-192150-7511https://doaj.org/article/d4340419f69e4fdc9a9f3aaecf1467ea2020-04-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.03197-19https://doaj.org/toc/2150-7511ABSTRACT A microfluidic system coupled with fluorescence microscopy is a powerful approach for quantitative analysis of bacterial growth. Here, we measure parameters of growth and dynamic localization of the cell division initiation protein FtsZ in Bacillus subtilis. Consistent with previous reports, we found that after division, FtsZ rings remain at the cell poles, and polar FtsZ ring disassembly coincides with rapid Z-ring accumulation at the midcell. In cells mutated for minD, however, the polar FtsZ rings persist indefinitely, suggesting that the primary function of the Min system is in Z-ring disassembly. The inability to recycle FtsZ monomers in the minD mutant results in the simultaneous maintenance of multiple Z-rings that are restricted by competition for newly synthesized FtsZ. Although the parameters of FtsZ dynamics change in the minD mutant, the overall cell division time remains the same, albeit with elongated cells necessary to accumulate a critical threshold amount of FtsZ for promoting medial division. Finally, the minD mutant characteristically produces minicells composed of polar peptidoglycan shown to be inert for remodeling in the wild type. Polar peptidoglycan, however, loses its inert character in the minD mutant, suggesting that the Min system not only is important for recycling FtsZ but also may have a secondary role in the spatiotemporal regulation of peptidoglycan remodeling. IMPORTANCE Many bacteria grow and divide by binary fission in which a mother cell divides into two identical daughter cells. To produce two equally sized daughters, the division machinery, guided by FtsZ, must dynamically localize to the midcell each cell cycle. Here, we quantitatively analyzed FtsZ dynamics during growth and found that the Min system of Bacillus subtilis is essential to disassemble FtsZ rings after division. Moreover, a failure to efficiently recycle FtsZ results in an increase in cell size. Finally, we show that the Min system has an additional role in inhibiting cell wall turnover and contributes to the “inert” property of cell walls at the poles.Yuanchen YuJinsheng ZhouFelix DempwolffJoshua D. BakerDaniel B. KearnsStephen C. JacobsonAmerican Society for MicrobiologyarticleFtsZMinDmicrofluidicsgrowthcell divisionpeptidoglycanMicrobiologyQR1-502ENmBio, Vol 11, Iss 2 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	FtsZ MinD microfluidics growth cell division peptidoglycan Microbiology QR1-502
spellingShingle	FtsZ MinD microfluidics growth cell division peptidoglycan Microbiology QR1-502 Yuanchen Yu Jinsheng Zhou Felix Dempwolff Joshua D. Baker Daniel B. Kearns Stephen C. Jacobson The Min System Disassembles FtsZ Foci and Inhibits Polar Peptidoglycan Remodeling in <named-content content-type="genus-species">Bacillus subtilis</named-content>
description	ABSTRACT A microfluidic system coupled with fluorescence microscopy is a powerful approach for quantitative analysis of bacterial growth. Here, we measure parameters of growth and dynamic localization of the cell division initiation protein FtsZ in Bacillus subtilis. Consistent with previous reports, we found that after division, FtsZ rings remain at the cell poles, and polar FtsZ ring disassembly coincides with rapid Z-ring accumulation at the midcell. In cells mutated for minD, however, the polar FtsZ rings persist indefinitely, suggesting that the primary function of the Min system is in Z-ring disassembly. The inability to recycle FtsZ monomers in the minD mutant results in the simultaneous maintenance of multiple Z-rings that are restricted by competition for newly synthesized FtsZ. Although the parameters of FtsZ dynamics change in the minD mutant, the overall cell division time remains the same, albeit with elongated cells necessary to accumulate a critical threshold amount of FtsZ for promoting medial division. Finally, the minD mutant characteristically produces minicells composed of polar peptidoglycan shown to be inert for remodeling in the wild type. Polar peptidoglycan, however, loses its inert character in the minD mutant, suggesting that the Min system not only is important for recycling FtsZ but also may have a secondary role in the spatiotemporal regulation of peptidoglycan remodeling. IMPORTANCE Many bacteria grow and divide by binary fission in which a mother cell divides into two identical daughter cells. To produce two equally sized daughters, the division machinery, guided by FtsZ, must dynamically localize to the midcell each cell cycle. Here, we quantitatively analyzed FtsZ dynamics during growth and found that the Min system of Bacillus subtilis is essential to disassemble FtsZ rings after division. Moreover, a failure to efficiently recycle FtsZ results in an increase in cell size. Finally, we show that the Min system has an additional role in inhibiting cell wall turnover and contributes to the “inert” property of cell walls at the poles.
format	article
author	Yuanchen Yu Jinsheng Zhou Felix Dempwolff Joshua D. Baker Daniel B. Kearns Stephen C. Jacobson
author_facet	Yuanchen Yu Jinsheng Zhou Felix Dempwolff Joshua D. Baker Daniel B. Kearns Stephen C. Jacobson
author_sort	Yuanchen Yu
title	The Min System Disassembles FtsZ Foci and Inhibits Polar Peptidoglycan Remodeling in <named-content content-type="genus-species">Bacillus subtilis</named-content>
title_short	The Min System Disassembles FtsZ Foci and Inhibits Polar Peptidoglycan Remodeling in <named-content content-type="genus-species">Bacillus subtilis</named-content>
title_full	The Min System Disassembles FtsZ Foci and Inhibits Polar Peptidoglycan Remodeling in <named-content content-type="genus-species">Bacillus subtilis</named-content>
title_fullStr	The Min System Disassembles FtsZ Foci and Inhibits Polar Peptidoglycan Remodeling in <named-content content-type="genus-species">Bacillus subtilis</named-content>
title_full_unstemmed	The Min System Disassembles FtsZ Foci and Inhibits Polar Peptidoglycan Remodeling in <named-content content-type="genus-species">Bacillus subtilis</named-content>
title_sort	min system disassembles ftsz foci and inhibits polar peptidoglycan remodeling in <named-content content-type="genus-species">bacillus subtilis</named-content>
publisher	American Society for Microbiology
publishDate	2020
url	https://doaj.org/article/d4340419f69e4fdc9a9f3aaecf1467ea
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The Min System Disassembles FtsZ Foci and Inhibits Polar Peptidoglycan Remodeling in <named-content content-type="genus-species">Bacillus subtilis</named-content>

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