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Inverse pH Regulation of Plant and Fungal Sucrose Transporters: A Mechanism to Regulate Competition for Sucrose at the Host/Pathogen Interface?
BACKGROUND: Plant sucrose transporter activities were shown to respond to changes in the extracellular pH and redox status, and oxidizing compounds like glutathione (GSSG) or H(2)O(2) were reported to effect the subcellular targeting of these proteins. We hypothesized that changes in both parameters...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
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Public Library of Science
2010
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2928750/ https://www.ncbi.nlm.nih.gov/pubmed/20865151 http://dx.doi.org/10.1371/journal.pone.0012429 |
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author | Wippel, Kathrin Wittek, Anke Hedrich, Rainer Sauer, Norbert |
author_facet | Wippel, Kathrin Wittek, Anke Hedrich, Rainer Sauer, Norbert |
author_sort | Wippel, Kathrin |
collection | PubMed |
description | BACKGROUND: Plant sucrose transporter activities were shown to respond to changes in the extracellular pH and redox status, and oxidizing compounds like glutathione (GSSG) or H(2)O(2) were reported to effect the subcellular targeting of these proteins. We hypothesized that changes in both parameters might be used to modulate the activities of competing sucrose transporters at a plant/pathogen interface. We, therefore, compared the effects of redox-active compounds and of extracellular pH on the sucrose transporters UmSRT1 and ZmSUT1 known to compete for extracellular sucrose in the Ustilago maydis (corn smut)/Zea mays (maize) pathosystem. METHODOLOGY/PRINCIPAL FINDINGS: We present functional analyses of the U. maydis sucrose transporter UmSRT1 and of the plant sucrose transporters ZmSUT1 and StSUT1 in Saccharomyces cerevisiae or in Xenopus laevis oocytes in the presence of different extracellular pH-values and redox systems, and study the possible effects of these treatments on the subcellular targeting. We observed an inverse regulation of host and pathogen sucrose transporters by changes in the apoplastic pH. Under none of the conditions analyzed, we could confirm the reported effects of redox-active compounds. CONCLUSIONS/SIGNIFICANCE: Our data suggest that changes in the extracellular pH but not of the extracellular redox status might be used to oppositely adjust the transport activities of plant and fungal sucrose transporters at the host/pathogen interface. |
format | Text |
id | pubmed-2928750 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-29287502010-09-23 Inverse pH Regulation of Plant and Fungal Sucrose Transporters: A Mechanism to Regulate Competition for Sucrose at the Host/Pathogen Interface? Wippel, Kathrin Wittek, Anke Hedrich, Rainer Sauer, Norbert PLoS One Research Article BACKGROUND: Plant sucrose transporter activities were shown to respond to changes in the extracellular pH and redox status, and oxidizing compounds like glutathione (GSSG) or H(2)O(2) were reported to effect the subcellular targeting of these proteins. We hypothesized that changes in both parameters might be used to modulate the activities of competing sucrose transporters at a plant/pathogen interface. We, therefore, compared the effects of redox-active compounds and of extracellular pH on the sucrose transporters UmSRT1 and ZmSUT1 known to compete for extracellular sucrose in the Ustilago maydis (corn smut)/Zea mays (maize) pathosystem. METHODOLOGY/PRINCIPAL FINDINGS: We present functional analyses of the U. maydis sucrose transporter UmSRT1 and of the plant sucrose transporters ZmSUT1 and StSUT1 in Saccharomyces cerevisiae or in Xenopus laevis oocytes in the presence of different extracellular pH-values and redox systems, and study the possible effects of these treatments on the subcellular targeting. We observed an inverse regulation of host and pathogen sucrose transporters by changes in the apoplastic pH. Under none of the conditions analyzed, we could confirm the reported effects of redox-active compounds. CONCLUSIONS/SIGNIFICANCE: Our data suggest that changes in the extracellular pH but not of the extracellular redox status might be used to oppositely adjust the transport activities of plant and fungal sucrose transporters at the host/pathogen interface. Public Library of Science 2010-08-26 /pmc/articles/PMC2928750/ /pubmed/20865151 http://dx.doi.org/10.1371/journal.pone.0012429 Text en Wippel et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Wippel, Kathrin Wittek, Anke Hedrich, Rainer Sauer, Norbert Inverse pH Regulation of Plant and Fungal Sucrose Transporters: A Mechanism to Regulate Competition for Sucrose at the Host/Pathogen Interface? |
title | Inverse pH Regulation of Plant and Fungal Sucrose Transporters: A Mechanism to Regulate Competition for Sucrose at the Host/Pathogen Interface? |
title_full | Inverse pH Regulation of Plant and Fungal Sucrose Transporters: A Mechanism to Regulate Competition for Sucrose at the Host/Pathogen Interface? |
title_fullStr | Inverse pH Regulation of Plant and Fungal Sucrose Transporters: A Mechanism to Regulate Competition for Sucrose at the Host/Pathogen Interface? |
title_full_unstemmed | Inverse pH Regulation of Plant and Fungal Sucrose Transporters: A Mechanism to Regulate Competition for Sucrose at the Host/Pathogen Interface? |
title_short | Inverse pH Regulation of Plant and Fungal Sucrose Transporters: A Mechanism to Regulate Competition for Sucrose at the Host/Pathogen Interface? |
title_sort | inverse ph regulation of plant and fungal sucrose transporters: a mechanism to regulate competition for sucrose at the host/pathogen interface? |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2928750/ https://www.ncbi.nlm.nih.gov/pubmed/20865151 http://dx.doi.org/10.1371/journal.pone.0012429 |
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