The role of the Cronobacter sakazakii ProP C-terminal coiled coil domain in osmotolerance

BACKGROUND: We investigate the role of the C-terminal coiled coil of the secondary proline porter ProP in contributing to Cronobacter sakazakii osmotolerance. FINDINGS: The extended C-terminal domain of ProP1 (encoded by ESA_02131) was spliced onto the truncated C-terminal end of ProP2 (encoded by E...

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Autores principales: Feeney, Audrey, Johnston, Christopher D, Lucid, Alan, O’Mahony, Jim, Coffey, Aidan, Lucey, Brigid, Sleator, Roy D
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2014
Materias:
Short Report
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4272814/
https://www.ncbi.nlm.nih.gov/pubmed/25530808
http://dx.doi.org/10.1186/s13099-014-0046-9
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author Feeney, Audrey
Johnston, Christopher D
Lucid, Alan
O’Mahony, Jim
Coffey, Aidan
Lucey, Brigid
Sleator, Roy D
author_facet Feeney, Audrey
Johnston, Christopher D
Lucid, Alan
O’Mahony, Jim
Coffey, Aidan
Lucey, Brigid
Sleator, Roy D
author_sort Feeney, Audrey
collection PubMed
description BACKGROUND: We investigate the role of the C-terminal coiled coil of the secondary proline porter ProP in contributing to Cronobacter sakazakii osmotolerance. FINDINGS: The extended C-terminal domain of ProP1 (encoded by ESA_02131) was spliced onto the truncated C-terminal end of ProP2 (encoded by ESA_01706); creating a chimeric protein (ProPc) which exhibits increased osmotolerance relative to the wild type. CONCLUSIONS: It appears that the C-terminal coiled coil domain tunes ProP at low osmolality, whereas ProP transporters lacking the coiled coil domain are more active at a higher osmolality range.
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spelling pubmed-42728142014-12-22 The role of the Cronobacter sakazakii ProP C-terminal coiled coil domain in osmotolerance Feeney, Audrey Johnston, Christopher D Lucid, Alan O’Mahony, Jim Coffey, Aidan Lucey, Brigid Sleator, Roy D Gut Pathog Short Report BACKGROUND: We investigate the role of the C-terminal coiled coil of the secondary proline porter ProP in contributing to Cronobacter sakazakii osmotolerance. FINDINGS: The extended C-terminal domain of ProP1 (encoded by ESA_02131) was spliced onto the truncated C-terminal end of ProP2 (encoded by ESA_01706); creating a chimeric protein (ProPc) which exhibits increased osmotolerance relative to the wild type. CONCLUSIONS: It appears that the C-terminal coiled coil domain tunes ProP at low osmolality, whereas ProP transporters lacking the coiled coil domain are more active at a higher osmolality range. BioMed Central 2014-12-16 /pmc/articles/PMC4272814/ /pubmed/25530808 http://dx.doi.org/10.1186/s13099-014-0046-9 Text en © Feeney et al.; licensee BioMed Central Ltd. 2014 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Short Report
Feeney, Audrey
Johnston, Christopher D
Lucid, Alan
O’Mahony, Jim
Coffey, Aidan
Lucey, Brigid
Sleator, Roy D
The role of the Cronobacter sakazakii ProP C-terminal coiled coil domain in osmotolerance
title The role of the Cronobacter sakazakii ProP C-terminal coiled coil domain in osmotolerance
title_full The role of the Cronobacter sakazakii ProP C-terminal coiled coil domain in osmotolerance
title_fullStr The role of the Cronobacter sakazakii ProP C-terminal coiled coil domain in osmotolerance
title_full_unstemmed The role of the Cronobacter sakazakii ProP C-terminal coiled coil domain in osmotolerance
title_short The role of the Cronobacter sakazakii ProP C-terminal coiled coil domain in osmotolerance
title_sort role of the cronobacter sakazakii prop c-terminal coiled coil domain in osmotolerance
topic Short Report
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4272814/
https://www.ncbi.nlm.nih.gov/pubmed/25530808
http://dx.doi.org/10.1186/s13099-014-0046-9
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