Cargando…
Intermembrane crosstalk drives inner-membrane protein organization in Escherichia coli
Gram-negative bacteria depend on energised protein complexes that connect the two membranes of the cell envelope. However, β-barrel outer-membrane proteins (OMPs) and α-helical inner-membrane proteins (IMPs) display quite different organisation. OMPs cluster into islands that restrict their lateral...
Autores principales: | , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5852019/ https://www.ncbi.nlm.nih.gov/pubmed/29540681 http://dx.doi.org/10.1038/s41467-018-03521-4 |
_version_ | 1783306479722299392 |
---|---|
author | Rassam, Patrice Long, Kathleen R. Kaminska, Renata Williams, David J. Papadakos, Grigorios Baumann, Christoph G. Kleanthous, Colin |
author_facet | Rassam, Patrice Long, Kathleen R. Kaminska, Renata Williams, David J. Papadakos, Grigorios Baumann, Christoph G. Kleanthous, Colin |
author_sort | Rassam, Patrice |
collection | PubMed |
description | Gram-negative bacteria depend on energised protein complexes that connect the two membranes of the cell envelope. However, β-barrel outer-membrane proteins (OMPs) and α-helical inner-membrane proteins (IMPs) display quite different organisation. OMPs cluster into islands that restrict their lateral mobility, while IMPs generally diffuse throughout the cell. Here, using live cell imaging of Escherichia coli, we demonstrate that when transient, energy-dependent transmembrane connections are formed, IMPs become subjugated by the inherent organisation of OMPs and that such connections impact IMP function. We show that while establishing a translocon for import, the colicin ColE9 sequesters the IMPs of the proton motive force (PMF)-linked Tol-Pal complex into islands mirroring those of colicin-bound OMPs. Through this imposed organisation, the bacteriocin subverts the outer-membrane stabilising role of Tol-Pal, blocking its recruitment to cell division sites and slowing membrane constriction. The ordering of IMPs by OMPs via an energised inter-membrane bridge represents an emerging functional paradigm in cell envelope biology. |
format | Online Article Text |
id | pubmed-5852019 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-58520192018-03-16 Intermembrane crosstalk drives inner-membrane protein organization in Escherichia coli Rassam, Patrice Long, Kathleen R. Kaminska, Renata Williams, David J. Papadakos, Grigorios Baumann, Christoph G. Kleanthous, Colin Nat Commun Article Gram-negative bacteria depend on energised protein complexes that connect the two membranes of the cell envelope. However, β-barrel outer-membrane proteins (OMPs) and α-helical inner-membrane proteins (IMPs) display quite different organisation. OMPs cluster into islands that restrict their lateral mobility, while IMPs generally diffuse throughout the cell. Here, using live cell imaging of Escherichia coli, we demonstrate that when transient, energy-dependent transmembrane connections are formed, IMPs become subjugated by the inherent organisation of OMPs and that such connections impact IMP function. We show that while establishing a translocon for import, the colicin ColE9 sequesters the IMPs of the proton motive force (PMF)-linked Tol-Pal complex into islands mirroring those of colicin-bound OMPs. Through this imposed organisation, the bacteriocin subverts the outer-membrane stabilising role of Tol-Pal, blocking its recruitment to cell division sites and slowing membrane constriction. The ordering of IMPs by OMPs via an energised inter-membrane bridge represents an emerging functional paradigm in cell envelope biology. Nature Publishing Group UK 2018-03-14 /pmc/articles/PMC5852019/ /pubmed/29540681 http://dx.doi.org/10.1038/s41467-018-03521-4 Text en © The Author(s) 2018 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 Rassam, Patrice Long, Kathleen R. Kaminska, Renata Williams, David J. Papadakos, Grigorios Baumann, Christoph G. Kleanthous, Colin Intermembrane crosstalk drives inner-membrane protein organization in Escherichia coli |
title | Intermembrane crosstalk drives inner-membrane protein organization in Escherichia coli |
title_full | Intermembrane crosstalk drives inner-membrane protein organization in Escherichia coli |
title_fullStr | Intermembrane crosstalk drives inner-membrane protein organization in Escherichia coli |
title_full_unstemmed | Intermembrane crosstalk drives inner-membrane protein organization in Escherichia coli |
title_short | Intermembrane crosstalk drives inner-membrane protein organization in Escherichia coli |
title_sort | intermembrane crosstalk drives inner-membrane protein organization in escherichia coli |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5852019/ https://www.ncbi.nlm.nih.gov/pubmed/29540681 http://dx.doi.org/10.1038/s41467-018-03521-4 |
work_keys_str_mv | AT rassampatrice intermembranecrosstalkdrivesinnermembraneproteinorganizationinescherichiacoli AT longkathleenr intermembranecrosstalkdrivesinnermembraneproteinorganizationinescherichiacoli AT kaminskarenata intermembranecrosstalkdrivesinnermembraneproteinorganizationinescherichiacoli AT williamsdavidj intermembranecrosstalkdrivesinnermembraneproteinorganizationinescherichiacoli AT papadakosgrigorios intermembranecrosstalkdrivesinnermembraneproteinorganizationinescherichiacoli AT baumannchristophg intermembranecrosstalkdrivesinnermembraneproteinorganizationinescherichiacoli AT kleanthouscolin intermembranecrosstalkdrivesinnermembraneproteinorganizationinescherichiacoli |