Changes of lipid domains in Bacillus subtilis cells with disrupted cell wall peptidoglycan

The cell wall is responsible for cell integrity and the maintenance of cell shape in bacteria. The Gram-positive bacterial cell wall consists of a thick peptidoglycan layer located on the outside of the cytoplasmic membrane. Bacterial cell membranes, like eukaryotic cell membranes, are known to cont...

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Main Authors:	Muchová, Katarína, Wilkinson, Anthony J, Barák, Imrich
Format:	Online
Language:	English
Published:	Blackwell Publishing Ltd 2011
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3433793/

id	pubmed-3433793
recordtype	oai_dc
spelling	pubmed-34337932012-09-06 Changes of lipid domains in Bacillus subtilis cells with disrupted cell wall peptidoglycan Muchová, Katarína Wilkinson, Anthony J Barák, Imrich Research Letters The cell wall is responsible for cell integrity and the maintenance of cell shape in bacteria. The Gram-positive bacterial cell wall consists of a thick peptidoglycan layer located on the outside of the cytoplasmic membrane. Bacterial cell membranes, like eukaryotic cell membranes, are known to contain domains of specific lipid and protein composition. Recently, using the membrane-binding fluorescent dye FM4-64, helix-like lipid structures extending along the long axis of the cell and consisting of negatively charged phospholipids were detected in the rod-shaped bacterium Bacillus subtilis. It was also shown that the cardiolipin-specific dye, nonyl acridine orange (NAO), is preferentially distributed at the cell poles and in the septal regions in both Escherichia coli and B. subtilis. These results suggest that phosphatidylglycerol is the principal component of the observed spiral domains in B. subtilis. Here, using the fluorescent dyes FM4-64 and NAO, we examined whether these lipid domains are linked to the presence of cell wall peptidoglycan. We show that in protoplasted cells, devoid of the peptidoglycan layer, helix-like lipid structures are not preserved. Specific lipid domains are also missing in cells depleted of MurG, an enzyme involved in peptidoglycan synthesis, indicating a link between lipid domain formation and peptidoglycan synthesis. Blackwell Publishing Ltd 2011-12 2011-10-03 /pmc/articles/PMC3433793/ /pubmed/22092867 http://dx.doi.org/10.1111/j.1574-6968.2011.02417.x Text en Copyright © 2011 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved http://creativecommons.org/licenses/by/2.5/ Re-use of this article is permitted in accordance with the Terms and Conditions set out at http://wileyonlinelibrary.com/onlineopen#OnlineOpen_Terms.
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Muchová, Katarína Wilkinson, Anthony J Barák, Imrich
spellingShingle	Muchová, Katarína Wilkinson, Anthony J Barák, Imrich Changes of lipid domains in Bacillus subtilis cells with disrupted cell wall peptidoglycan
author_facet	Muchová, Katarína Wilkinson, Anthony J Barák, Imrich
author_sort	Muchová, Katarína
title	Changes of lipid domains in Bacillus subtilis cells with disrupted cell wall peptidoglycan
title_short	Changes of lipid domains in Bacillus subtilis cells with disrupted cell wall peptidoglycan
title_full	Changes of lipid domains in Bacillus subtilis cells with disrupted cell wall peptidoglycan
title_fullStr	Changes of lipid domains in Bacillus subtilis cells with disrupted cell wall peptidoglycan
title_full_unstemmed	Changes of lipid domains in Bacillus subtilis cells with disrupted cell wall peptidoglycan
title_sort	changes of lipid domains in bacillus subtilis cells with disrupted cell wall peptidoglycan
description	The cell wall is responsible for cell integrity and the maintenance of cell shape in bacteria. The Gram-positive bacterial cell wall consists of a thick peptidoglycan layer located on the outside of the cytoplasmic membrane. Bacterial cell membranes, like eukaryotic cell membranes, are known to contain domains of specific lipid and protein composition. Recently, using the membrane-binding fluorescent dye FM4-64, helix-like lipid structures extending along the long axis of the cell and consisting of negatively charged phospholipids were detected in the rod-shaped bacterium Bacillus subtilis. It was also shown that the cardiolipin-specific dye, nonyl acridine orange (NAO), is preferentially distributed at the cell poles and in the septal regions in both Escherichia coli and B. subtilis. These results suggest that phosphatidylglycerol is the principal component of the observed spiral domains in B. subtilis. Here, using the fluorescent dyes FM4-64 and NAO, we examined whether these lipid domains are linked to the presence of cell wall peptidoglycan. We show that in protoplasted cells, devoid of the peptidoglycan layer, helix-like lipid structures are not preserved. Specific lipid domains are also missing in cells depleted of MurG, an enzyme involved in peptidoglycan synthesis, indicating a link between lipid domain formation and peptidoglycan synthesis.
publisher	Blackwell Publishing Ltd
publishDate	2011
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3433793/
_version_	1611554189757906944

Changes of lipid domains in Bacillus subtilis cells with disrupted cell wall peptidoglycan

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