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The Role of the Small Export Apparatus Protein, SctS, in the Activity of the Type III Secretion System
Many gram-negative pathogens utilize a protein complex, termed the type III secretion system (T3SS), to inject virulence factors from their cytoplasm directly into the host cell. An export apparatus that is formed by five putative integral membrane proteins (SctR/S/T/U/V), resides at the center of t...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6863770/ https://www.ncbi.nlm.nih.gov/pubmed/31798543 http://dx.doi.org/10.3389/fmicb.2019.02551 |
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author | Tseytin, Irit Mitrovic, Bosko David, Nofar Langenfeld, Katja Zarivach, Raz Diepold, Andreas Sal-Man, Neta |
author_facet | Tseytin, Irit Mitrovic, Bosko David, Nofar Langenfeld, Katja Zarivach, Raz Diepold, Andreas Sal-Man, Neta |
author_sort | Tseytin, Irit |
collection | PubMed |
description | Many gram-negative pathogens utilize a protein complex, termed the type III secretion system (T3SS), to inject virulence factors from their cytoplasm directly into the host cell. An export apparatus that is formed by five putative integral membrane proteins (SctR/S/T/U/V), resides at the center of the T3SS complex. In this study, we characterized the smallest export apparatus protein, SctS, which contains two putative transmembrane domains (PTMD) that dynamically extract from the inner membrane and adopt a helix-turn-helix structure upon assembly of the T3SS. Replacement of each SctS PTMD with an alternative hydrophobic sequence resulted in abolishment of the T3SS activity, yet SctS self- and hetero-interactions as well as the overall assembly of the T3SS complex were unaffected. Our findings suggest that SctS PTMDs are not crucial for the interactions or the assembly of the T3SS base complex but rather that they are involved in adjusting the orientation of the export apparatus relative to additional T3SS sub-structures, such as the cytoplasmic- and the inner-membrane rings. This ensures the fittings between the dynamic and static components of the T3SS and supports the functionality of the T3SS complex. |
format | Online Article Text |
id | pubmed-6863770 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-68637702019-12-03 The Role of the Small Export Apparatus Protein, SctS, in the Activity of the Type III Secretion System Tseytin, Irit Mitrovic, Bosko David, Nofar Langenfeld, Katja Zarivach, Raz Diepold, Andreas Sal-Man, Neta Front Microbiol Microbiology Many gram-negative pathogens utilize a protein complex, termed the type III secretion system (T3SS), to inject virulence factors from their cytoplasm directly into the host cell. An export apparatus that is formed by five putative integral membrane proteins (SctR/S/T/U/V), resides at the center of the T3SS complex. In this study, we characterized the smallest export apparatus protein, SctS, which contains two putative transmembrane domains (PTMD) that dynamically extract from the inner membrane and adopt a helix-turn-helix structure upon assembly of the T3SS. Replacement of each SctS PTMD with an alternative hydrophobic sequence resulted in abolishment of the T3SS activity, yet SctS self- and hetero-interactions as well as the overall assembly of the T3SS complex were unaffected. Our findings suggest that SctS PTMDs are not crucial for the interactions or the assembly of the T3SS base complex but rather that they are involved in adjusting the orientation of the export apparatus relative to additional T3SS sub-structures, such as the cytoplasmic- and the inner-membrane rings. This ensures the fittings between the dynamic and static components of the T3SS and supports the functionality of the T3SS complex. Frontiers Media S.A. 2019-11-13 /pmc/articles/PMC6863770/ /pubmed/31798543 http://dx.doi.org/10.3389/fmicb.2019.02551 Text en Copyright © 2019 Tseytin, Mitrovic, David, Langenfeld, Zarivach, Diepold and Sal-Man. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Microbiology Tseytin, Irit Mitrovic, Bosko David, Nofar Langenfeld, Katja Zarivach, Raz Diepold, Andreas Sal-Man, Neta The Role of the Small Export Apparatus Protein, SctS, in the Activity of the Type III Secretion System |
title | The Role of the Small Export Apparatus Protein, SctS, in the Activity of the Type III Secretion System |
title_full | The Role of the Small Export Apparatus Protein, SctS, in the Activity of the Type III Secretion System |
title_fullStr | The Role of the Small Export Apparatus Protein, SctS, in the Activity of the Type III Secretion System |
title_full_unstemmed | The Role of the Small Export Apparatus Protein, SctS, in the Activity of the Type III Secretion System |
title_short | The Role of the Small Export Apparatus Protein, SctS, in the Activity of the Type III Secretion System |
title_sort | role of the small export apparatus protein, scts, in the activity of the type iii secretion system |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6863770/ https://www.ncbi.nlm.nih.gov/pubmed/31798543 http://dx.doi.org/10.3389/fmicb.2019.02551 |
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