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In vivo quantification of the secretion rates of the hemolysin A Type I secretion system

Type 1 secretion systems (T1SS) of Gram-negative bacteria secrete a broad range of substrates into the extracellular space. Common to all substrates is a C-terminal secretion sequence and nonapeptide repeats in the C-terminal part that bind Ca(2+) in the extracellular space, to trigger protein foldi...

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Autores principales: Lenders, Michael H. H., Beer, Tobias, Smits, Sander H. J., Schmitt, Lutz
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5018854/
https://www.ncbi.nlm.nih.gov/pubmed/27616645
http://dx.doi.org/10.1038/srep33275
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author Lenders, Michael H. H.
Beer, Tobias
Smits, Sander H. J.
Schmitt, Lutz
author_facet Lenders, Michael H. H.
Beer, Tobias
Smits, Sander H. J.
Schmitt, Lutz
author_sort Lenders, Michael H. H.
collection PubMed
description Type 1 secretion systems (T1SS) of Gram-negative bacteria secrete a broad range of substrates into the extracellular space. Common to all substrates is a C-terminal secretion sequence and nonapeptide repeats in the C-terminal part that bind Ca(2+) in the extracellular space, to trigger protein folding. Like all T1SS, the hemolysin A (HlyA) T1SS of Escherichia coli consists of an ABC transporter, a membrane fusion protein and an outer membrane protein allowing the one step translocation of the substrate across both membranes. Here, we analyzed the secretion rate of the HlyA T1SS. Our results demonstrate that the rate is independent of substrate-size and operates at a speed of approximately 16 amino acids per transporter per second. We also demonstrate that the rate is independent of the extracellular Ca(2+) concentration raising the question of the driving force of substrate secretion by T1SS in general.
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spelling pubmed-50188542016-09-19 In vivo quantification of the secretion rates of the hemolysin A Type I secretion system Lenders, Michael H. H. Beer, Tobias Smits, Sander H. J. Schmitt, Lutz Sci Rep Article Type 1 secretion systems (T1SS) of Gram-negative bacteria secrete a broad range of substrates into the extracellular space. Common to all substrates is a C-terminal secretion sequence and nonapeptide repeats in the C-terminal part that bind Ca(2+) in the extracellular space, to trigger protein folding. Like all T1SS, the hemolysin A (HlyA) T1SS of Escherichia coli consists of an ABC transporter, a membrane fusion protein and an outer membrane protein allowing the one step translocation of the substrate across both membranes. Here, we analyzed the secretion rate of the HlyA T1SS. Our results demonstrate that the rate is independent of substrate-size and operates at a speed of approximately 16 amino acids per transporter per second. We also demonstrate that the rate is independent of the extracellular Ca(2+) concentration raising the question of the driving force of substrate secretion by T1SS in general. Nature Publishing Group 2016-09-12 /pmc/articles/PMC5018854/ /pubmed/27616645 http://dx.doi.org/10.1038/srep33275 Text en Copyright © 2016, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
Lenders, Michael H. H.
Beer, Tobias
Smits, Sander H. J.
Schmitt, Lutz
In vivo quantification of the secretion rates of the hemolysin A Type I secretion system
title In vivo quantification of the secretion rates of the hemolysin A Type I secretion system
title_full In vivo quantification of the secretion rates of the hemolysin A Type I secretion system
title_fullStr In vivo quantification of the secretion rates of the hemolysin A Type I secretion system
title_full_unstemmed In vivo quantification of the secretion rates of the hemolysin A Type I secretion system
title_short In vivo quantification of the secretion rates of the hemolysin A Type I secretion system
title_sort in vivo quantification of the secretion rates of the hemolysin a type i secretion system
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5018854/
https://www.ncbi.nlm.nih.gov/pubmed/27616645
http://dx.doi.org/10.1038/srep33275
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