Membrane interactions and self‐association of components of the Ess/Type VII secretion system of Staphylococcus aureus

The Ess/Type VII protein secretion system, essential for virulence of pathogenic Staphylococcus aureus, is dependent upon the four core membrane proteins EssA, EssB, EssC and EsaA. Here, we use crosslinking and blue native PAGE analysis to show that the EssB, EssC and EsaA proteins individually form...

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Autores principales: Jäger, Franziska, Zoltner, Martin, Kneuper, Holger, Hunter, William N., Palmer, Tracy
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2016
Materias:
Research Letters
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4949537/
https://www.ncbi.nlm.nih.gov/pubmed/26785823
http://dx.doi.org/10.1002/1873-3468.12065
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author Jäger, Franziska
Zoltner, Martin
Kneuper, Holger
Hunter, William N.
Palmer, Tracy
author_facet Jäger, Franziska
Zoltner, Martin
Kneuper, Holger
Hunter, William N.
Palmer, Tracy
author_sort Jäger, Franziska
collection PubMed
description The Ess/Type VII protein secretion system, essential for virulence of pathogenic Staphylococcus aureus, is dependent upon the four core membrane proteins EssA, EssB, EssC and EsaA. Here, we use crosslinking and blue native PAGE analysis to show that the EssB, EssC and EsaA proteins individually form homomeric complexes. Surprisingly, these components appear unable to interact with each other, or with the EssA protein. We further show that two high molecular weight multimers of EssC detected in whole cells are not dependent upon the presence of EsxA, EsxB or any other Ess component for their assembly.
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spelling pubmed-49495372016-07-28 Membrane interactions and self‐association of components of the Ess/Type VII secretion system of Staphylococcus aureus Jäger, Franziska Zoltner, Martin Kneuper, Holger Hunter, William N. Palmer, Tracy FEBS Lett Research Letters The Ess/Type VII protein secretion system, essential for virulence of pathogenic Staphylococcus aureus, is dependent upon the four core membrane proteins EssA, EssB, EssC and EsaA. Here, we use crosslinking and blue native PAGE analysis to show that the EssB, EssC and EsaA proteins individually form homomeric complexes. Surprisingly, these components appear unable to interact with each other, or with the EssA protein. We further show that two high molecular weight multimers of EssC detected in whole cells are not dependent upon the presence of EsxA, EsxB or any other Ess component for their assembly. John Wiley and Sons Inc. 2016-02-03 2016-02 /pmc/articles/PMC4949537/ /pubmed/26785823 http://dx.doi.org/10.1002/1873-3468.12065 Text en © 2016 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies. This is an open access article under the terms of the Creative Commons Attribution (http://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Letters
Jäger, Franziska
Zoltner, Martin
Kneuper, Holger
Hunter, William N.
Palmer, Tracy
Membrane interactions and self‐association of components of the Ess/Type VII secretion system of Staphylococcus aureus
title Membrane interactions and self‐association of components of the Ess/Type VII secretion system of Staphylococcus aureus
title_full Membrane interactions and self‐association of components of the Ess/Type VII secretion system of Staphylococcus aureus
title_fullStr Membrane interactions and self‐association of components of the Ess/Type VII secretion system of Staphylococcus aureus
title_full_unstemmed Membrane interactions and self‐association of components of the Ess/Type VII secretion system of Staphylococcus aureus
title_short Membrane interactions and self‐association of components of the Ess/Type VII secretion system of Staphylococcus aureus
title_sort membrane interactions and self‐association of components of the ess/type vii secretion system of staphylococcus aureus
topic Research Letters
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4949537/
https://www.ncbi.nlm.nih.gov/pubmed/26785823
http://dx.doi.org/10.1002/1873-3468.12065
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