The <i>Escherichia coli</i> Outer Membrane β-Barrel Assembly Machinery (BAM) Crosstalks with the Divisome

The BAM is a macromolecular machine responsible for the folding and the insertion of integral proteins into the outer membrane of diderm Gram-negative bacteria. In <i>Escherichia coli</i>, it consists of a transmembrane β-barrel subunit, BamA, and four outer membrane lipoproteins (BamB-E...

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Autores principales:	Elisa Consoli, Joen Luirink, Tanneke den Blaauwen
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	<i>Escherichia coli</i> β-barrel assembly machinery BAM complex divisome Sec machinery immunolabelling Biology (General) QH301-705.5 Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/87430181f226430d92a552dd85275b93
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spelling	oai:doaj.org-article:87430181f226430d92a552dd85275b932021-11-25T17:53:25ZThe <i>Escherichia coli</i> Outer Membrane β-Barrel Assembly Machinery (BAM) Crosstalks with the Divisome10.3390/ijms2222121011422-00671661-6596https://doaj.org/article/87430181f226430d92a552dd85275b932021-11-01T00:00:00Zhttps://www.mdpi.com/1422-0067/22/22/12101https://doaj.org/toc/1661-6596https://doaj.org/toc/1422-0067The BAM is a macromolecular machine responsible for the folding and the insertion of integral proteins into the outer membrane of diderm Gram-negative bacteria. In <i>Escherichia coli</i>, it consists of a transmembrane β-barrel subunit, BamA, and four outer membrane lipoproteins (BamB-E). Using BAM-specific antibodies, in <i>E. coli</i> cells, the complex is shown to localize in the lateral wall in foci. The machinery was shown to be enriched at midcell with specific cell cycle timing. The inhibition of septation by aztreonam did not alter the BAM midcell localization substantially. Furthermore, the absence of late cell division proteins at midcell did not impact BAM timing or localization. These results imply that the BAM enrichment at the site of constriction does not require an active cell division machinery. Expression of the Tre1 toxin, which impairs the FtsZ filamentation and therefore midcell localization, resulted in the complete loss of BAM midcell enrichment. A similar effect was observed for YidC, which is involved in the membrane insertion of cell division proteins in the inner membrane. The presence of the Z-ring is needed for preseptal peptidoglycan (PG) synthesis. As BAM was shown to be embedded in the PG layer, it is possible that BAM is inserted preferentially simultaneously with de novo PG synthesis to facilitate the insertion of OMPs in the newly synthesized outer membrane.Elisa ConsoliJoen LuirinkTanneke den BlaauwenMDPI AGarticle<i>Escherichia coli</i>β-barrel assembly machineryBAM complexdivisomeSec machineryimmunolabellingBiology (General)QH301-705.5ChemistryQD1-999ENInternational Journal of Molecular Sciences, Vol 22, Iss 12101, p 12101 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	<i>Escherichia coli</i> β-barrel assembly machinery BAM complex divisome Sec machinery immunolabelling Biology (General) QH301-705.5 Chemistry QD1-999
spellingShingle	<i>Escherichia coli</i> β-barrel assembly machinery BAM complex divisome Sec machinery immunolabelling Biology (General) QH301-705.5 Chemistry QD1-999 Elisa Consoli Joen Luirink Tanneke den Blaauwen The <i>Escherichia coli</i> Outer Membrane β-Barrel Assembly Machinery (BAM) Crosstalks with the Divisome
description	The BAM is a macromolecular machine responsible for the folding and the insertion of integral proteins into the outer membrane of diderm Gram-negative bacteria. In <i>Escherichia coli</i>, it consists of a transmembrane β-barrel subunit, BamA, and four outer membrane lipoproteins (BamB-E). Using BAM-specific antibodies, in <i>E. coli</i> cells, the complex is shown to localize in the lateral wall in foci. The machinery was shown to be enriched at midcell with specific cell cycle timing. The inhibition of septation by aztreonam did not alter the BAM midcell localization substantially. Furthermore, the absence of late cell division proteins at midcell did not impact BAM timing or localization. These results imply that the BAM enrichment at the site of constriction does not require an active cell division machinery. Expression of the Tre1 toxin, which impairs the FtsZ filamentation and therefore midcell localization, resulted in the complete loss of BAM midcell enrichment. A similar effect was observed for YidC, which is involved in the membrane insertion of cell division proteins in the inner membrane. The presence of the Z-ring is needed for preseptal peptidoglycan (PG) synthesis. As BAM was shown to be embedded in the PG layer, it is possible that BAM is inserted preferentially simultaneously with de novo PG synthesis to facilitate the insertion of OMPs in the newly synthesized outer membrane.
format	article
author	Elisa Consoli Joen Luirink Tanneke den Blaauwen
author_facet	Elisa Consoli Joen Luirink Tanneke den Blaauwen
author_sort	Elisa Consoli
title	The <i>Escherichia coli</i> Outer Membrane β-Barrel Assembly Machinery (BAM) Crosstalks with the Divisome
title_short	The <i>Escherichia coli</i> Outer Membrane β-Barrel Assembly Machinery (BAM) Crosstalks with the Divisome
title_full	The <i>Escherichia coli</i> Outer Membrane β-Barrel Assembly Machinery (BAM) Crosstalks with the Divisome
title_fullStr	The <i>Escherichia coli</i> Outer Membrane β-Barrel Assembly Machinery (BAM) Crosstalks with the Divisome
title_full_unstemmed	The <i>Escherichia coli</i> Outer Membrane β-Barrel Assembly Machinery (BAM) Crosstalks with the Divisome
title_sort	<i>escherichia coli</i> outer membrane β-barrel assembly machinery (bam) crosstalks with the divisome
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/87430181f226430d92a552dd85275b93
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The <i>Escherichia coli</i> Outer Membrane β-Barrel Assembly Machinery (BAM) Crosstalks with the Divisome

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