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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...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2020
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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. |
format | Online Article Text |
id | pubmed-7066135 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
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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