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Contribution of mechanosensitive channels to osmoadaptation and ectoine excretion in Halomonas elongata

For osmoadaptation the halophilic bacterium Halomonas elongata synthesizes as its main compatible solute the aspartate derivative ectoine. H. elongata does not rely entirely on synthesis but can accumulate ectoine by uptake from the surrounding environment with the help of the osmoregulated transpor...

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Autores principales: Vandrich, Jasmina, Pfeiffer, Friedhelm, Alfaro-Espinoza, Gabriela, Kunte, Hans Jörg
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Japan 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7174268/
https://www.ncbi.nlm.nih.gov/pubmed/32266565
http://dx.doi.org/10.1007/s00792-020-01168-y
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author Vandrich, Jasmina
Pfeiffer, Friedhelm
Alfaro-Espinoza, Gabriela
Kunte, Hans Jörg
author_facet Vandrich, Jasmina
Pfeiffer, Friedhelm
Alfaro-Espinoza, Gabriela
Kunte, Hans Jörg
author_sort Vandrich, Jasmina
collection PubMed
description For osmoadaptation the halophilic bacterium Halomonas elongata synthesizes as its main compatible solute the aspartate derivative ectoine. H. elongata does not rely entirely on synthesis but can accumulate ectoine by uptake from the surrounding environment with the help of the osmoregulated transporter TeaABC. Disruption of the TeaABC-mediated ectoine uptake creates a strain that is constantly losing ectoine to the medium. However, the efflux mechanism of ectoine in H. elongata is not yet understood. H. elongata possesses four genes encoding mechanosensitive channels all of which belong to the small conductance type (MscS). Analysis by qRT-PCR revealed a reduction in transcription of the mscS genes with increasing salinity. The response of H. elongata to hypo- and hyperosmotic shock never resulted in up-regulation but rather in down-regulation of mscS transcription. Deletion of all four mscS genes created a mutant that was unable to cope with hypoosmotic shock. However, the knockout mutant grew significantly faster than the wildtype at high salinity of 2 M NaCl, and most importantly, still exported 80% of the ectoine compared to the wildtype. We thus conclude that a yet unknown system, which is independent of mechanosensitive channels, is the major export route for ectoine in H. elongata. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s00792-020-01168-y) contains supplementary material, which is available to authorized users.
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spelling pubmed-71742682020-04-23 Contribution of mechanosensitive channels to osmoadaptation and ectoine excretion in Halomonas elongata Vandrich, Jasmina Pfeiffer, Friedhelm Alfaro-Espinoza, Gabriela Kunte, Hans Jörg Extremophiles Original Paper For osmoadaptation the halophilic bacterium Halomonas elongata synthesizes as its main compatible solute the aspartate derivative ectoine. H. elongata does not rely entirely on synthesis but can accumulate ectoine by uptake from the surrounding environment with the help of the osmoregulated transporter TeaABC. Disruption of the TeaABC-mediated ectoine uptake creates a strain that is constantly losing ectoine to the medium. However, the efflux mechanism of ectoine in H. elongata is not yet understood. H. elongata possesses four genes encoding mechanosensitive channels all of which belong to the small conductance type (MscS). Analysis by qRT-PCR revealed a reduction in transcription of the mscS genes with increasing salinity. The response of H. elongata to hypo- and hyperosmotic shock never resulted in up-regulation but rather in down-regulation of mscS transcription. Deletion of all four mscS genes created a mutant that was unable to cope with hypoosmotic shock. However, the knockout mutant grew significantly faster than the wildtype at high salinity of 2 M NaCl, and most importantly, still exported 80% of the ectoine compared to the wildtype. We thus conclude that a yet unknown system, which is independent of mechanosensitive channels, is the major export route for ectoine in H. elongata. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s00792-020-01168-y) contains supplementary material, which is available to authorized users. Springer Japan 2020-04-07 2020 /pmc/articles/PMC7174268/ /pubmed/32266565 http://dx.doi.org/10.1007/s00792-020-01168-y Text en © The Author(s) 2020 Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Original Paper
Vandrich, Jasmina
Pfeiffer, Friedhelm
Alfaro-Espinoza, Gabriela
Kunte, Hans Jörg
Contribution of mechanosensitive channels to osmoadaptation and ectoine excretion in Halomonas elongata
title Contribution of mechanosensitive channels to osmoadaptation and ectoine excretion in Halomonas elongata
title_full Contribution of mechanosensitive channels to osmoadaptation and ectoine excretion in Halomonas elongata
title_fullStr Contribution of mechanosensitive channels to osmoadaptation and ectoine excretion in Halomonas elongata
title_full_unstemmed Contribution of mechanosensitive channels to osmoadaptation and ectoine excretion in Halomonas elongata
title_short Contribution of mechanosensitive channels to osmoadaptation and ectoine excretion in Halomonas elongata
title_sort contribution of mechanosensitive channels to osmoadaptation and ectoine excretion in halomonas elongata
topic Original Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7174268/
https://www.ncbi.nlm.nih.gov/pubmed/32266565
http://dx.doi.org/10.1007/s00792-020-01168-y
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