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Heterogeneous localisation of membrane proteins in Staphylococcus aureus
The bacterial cytoplasmic membrane is the interface between the cell and its environment, with multiple membrane proteins serving its many functions. However, how these proteins are organised to permit optimal physiological processes is largely unknown. Based on our initial findings that 2 phospholi...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5826919/ https://www.ncbi.nlm.nih.gov/pubmed/29483609 http://dx.doi.org/10.1038/s41598-018-21750-x |
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author | Weihs, Felix Wacnik, Katarzyna Turner, Robert D. Culley, Siân Henriques, Ricardo Foster, Simon J. |
author_facet | Weihs, Felix Wacnik, Katarzyna Turner, Robert D. Culley, Siân Henriques, Ricardo Foster, Simon J. |
author_sort | Weihs, Felix |
collection | PubMed |
description | The bacterial cytoplasmic membrane is the interface between the cell and its environment, with multiple membrane proteins serving its many functions. However, how these proteins are organised to permit optimal physiological processes is largely unknown. Based on our initial findings that 2 phospholipid biosynthetic enzymes (PlsY and CdsA) localise heterogeneously in the membrane of the bacterium Staphylococcus aureus, we have analysed the localisation of other key membrane proteins. A range of protein fusions were constructed and used in conjunction with quantitative image analysis. Enzymes involved in phospholipid biosynthesis as well as the lipid raft marker FloT exhibited a heterogeneous localisation pattern. However, the secretion associated SecY protein, was more homogeneously distributed in the membrane. A FRET-based system also identified novel colocalisation between phospholipid biosynthesis enzymes and the respiratory protein CydB revealing a likely larger network of partners. PlsY localisation was found to be dose dependent but not to be affected by membrane lipid composition. Disruption of the activity of the essential cell division organiser FtsZ, using the inhibitor PC190723 led to loss of PlsY localisation, revealing a link to cell division and a possible role for FtsZ in functions not strictly associated with septum formation. |
format | Online Article Text |
id | pubmed-5826919 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-58269192018-03-01 Heterogeneous localisation of membrane proteins in Staphylococcus aureus Weihs, Felix Wacnik, Katarzyna Turner, Robert D. Culley, Siân Henriques, Ricardo Foster, Simon J. Sci Rep Article The bacterial cytoplasmic membrane is the interface between the cell and its environment, with multiple membrane proteins serving its many functions. However, how these proteins are organised to permit optimal physiological processes is largely unknown. Based on our initial findings that 2 phospholipid biosynthetic enzymes (PlsY and CdsA) localise heterogeneously in the membrane of the bacterium Staphylococcus aureus, we have analysed the localisation of other key membrane proteins. A range of protein fusions were constructed and used in conjunction with quantitative image analysis. Enzymes involved in phospholipid biosynthesis as well as the lipid raft marker FloT exhibited a heterogeneous localisation pattern. However, the secretion associated SecY protein, was more homogeneously distributed in the membrane. A FRET-based system also identified novel colocalisation between phospholipid biosynthesis enzymes and the respiratory protein CydB revealing a likely larger network of partners. PlsY localisation was found to be dose dependent but not to be affected by membrane lipid composition. Disruption of the activity of the essential cell division organiser FtsZ, using the inhibitor PC190723 led to loss of PlsY localisation, revealing a link to cell division and a possible role for FtsZ in functions not strictly associated with septum formation. Nature Publishing Group UK 2018-02-26 /pmc/articles/PMC5826919/ /pubmed/29483609 http://dx.doi.org/10.1038/s41598-018-21750-x 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 Weihs, Felix Wacnik, Katarzyna Turner, Robert D. Culley, Siân Henriques, Ricardo Foster, Simon J. Heterogeneous localisation of membrane proteins in Staphylococcus aureus |
title | Heterogeneous localisation of membrane proteins in Staphylococcus aureus |
title_full | Heterogeneous localisation of membrane proteins in Staphylococcus aureus |
title_fullStr | Heterogeneous localisation of membrane proteins in Staphylococcus aureus |
title_full_unstemmed | Heterogeneous localisation of membrane proteins in Staphylococcus aureus |
title_short | Heterogeneous localisation of membrane proteins in Staphylococcus aureus |
title_sort | heterogeneous localisation of membrane proteins in staphylococcus aureus |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5826919/ https://www.ncbi.nlm.nih.gov/pubmed/29483609 http://dx.doi.org/10.1038/s41598-018-21750-x |
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