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The lipoprotein Pal stabilises the bacterial outer membrane during constriction by a mobilisation-and-capture mechanism

Coordination of outer membrane constriction with septation is critical to faithful division in Gram-negative bacteria and vital to the barrier function of the membrane. This coordination requires the recruitment of the peptidoglycan-binding outer-membrane lipoprotein Pal at division sites by the Tol...

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Autores principales: Szczepaniak, Joanna, Holmes, Peter, Rajasekar, Karthik, Kaminska, Renata, Samsudin, Firdaus, Inns, Patrick George, Rassam, Patrice, Khalid, Syma, Murray, Seán M., Redfield, Christina, Kleanthous, Colin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7066135/
https://www.ncbi.nlm.nih.gov/pubmed/32161270
http://dx.doi.org/10.1038/s41467-020-15083-5
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author Szczepaniak, Joanna
Holmes, Peter
Rajasekar, Karthik
Kaminska, Renata
Samsudin, Firdaus
Inns, Patrick George
Rassam, Patrice
Khalid, Syma
Murray, Seán M.
Redfield, Christina
Kleanthous, Colin
author_facet Szczepaniak, Joanna
Holmes, Peter
Rajasekar, Karthik
Kaminska, Renata
Samsudin, Firdaus
Inns, Patrick George
Rassam, Patrice
Khalid, Syma
Murray, Seán M.
Redfield, Christina
Kleanthous, Colin
author_sort Szczepaniak, Joanna
collection PubMed
description Coordination of outer membrane constriction with septation is critical to faithful division in Gram-negative bacteria and vital to the barrier function of the membrane. This coordination requires the recruitment of the peptidoglycan-binding outer-membrane lipoprotein Pal at division sites by the Tol system. Here, we show that Pal accumulation at Escherichia coli division sites is a consequence of three key functions of the Tol system. First, Tol mobilises Pal molecules in dividing cells, which otherwise diffuse very slowly due to their binding of the cell wall. Second, Tol actively captures mobilised Pal molecules and deposits them at the division septum. Third, the active capture mechanism is analogous to that used by the inner membrane protein TonB to dislodge the plug domains of outer membrane TonB-dependent nutrient transporters. We conclude that outer membrane constriction is coordinated with cell division by active mobilisation-and-capture of Pal at division septa by the Tol system.
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spelling pubmed-70661352020-03-18 The lipoprotein Pal stabilises the bacterial outer membrane during constriction by a mobilisation-and-capture mechanism Szczepaniak, Joanna Holmes, Peter Rajasekar, Karthik Kaminska, Renata Samsudin, Firdaus Inns, Patrick George Rassam, Patrice Khalid, Syma Murray, Seán M. Redfield, Christina Kleanthous, Colin Nat Commun Article Coordination of outer membrane constriction with septation is critical to faithful division in Gram-negative bacteria and vital to the barrier function of the membrane. This coordination requires the recruitment of the peptidoglycan-binding outer-membrane lipoprotein Pal at division sites by the Tol system. Here, we show that Pal accumulation at Escherichia coli division sites is a consequence of three key functions of the Tol system. First, Tol mobilises Pal molecules in dividing cells, which otherwise diffuse very slowly due to their binding of the cell wall. Second, Tol actively captures mobilised Pal molecules and deposits them at the division septum. Third, the active capture mechanism is analogous to that used by the inner membrane protein TonB to dislodge the plug domains of outer membrane TonB-dependent nutrient transporters. We conclude that outer membrane constriction is coordinated with cell division by active mobilisation-and-capture of Pal at division septa by the Tol system. Nature Publishing Group UK 2020-03-11 /pmc/articles/PMC7066135/ /pubmed/32161270 http://dx.doi.org/10.1038/s41467-020-15083-5 Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Szczepaniak, Joanna
Holmes, Peter
Rajasekar, Karthik
Kaminska, Renata
Samsudin, Firdaus
Inns, Patrick George
Rassam, Patrice
Khalid, Syma
Murray, Seán M.
Redfield, Christina
Kleanthous, Colin
The lipoprotein Pal stabilises the bacterial outer membrane during constriction by a mobilisation-and-capture mechanism
title The lipoprotein Pal stabilises the bacterial outer membrane during constriction by a mobilisation-and-capture mechanism
title_full The lipoprotein Pal stabilises the bacterial outer membrane during constriction by a mobilisation-and-capture mechanism
title_fullStr The lipoprotein Pal stabilises the bacterial outer membrane during constriction by a mobilisation-and-capture mechanism
title_full_unstemmed The lipoprotein Pal stabilises the bacterial outer membrane during constriction by a mobilisation-and-capture mechanism
title_short The lipoprotein Pal stabilises the bacterial outer membrane during constriction by a mobilisation-and-capture mechanism
title_sort lipoprotein pal stabilises the bacterial outer membrane during constriction by a mobilisation-and-capture mechanism
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7066135/
https://www.ncbi.nlm.nih.gov/pubmed/32161270
http://dx.doi.org/10.1038/s41467-020-15083-5
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