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Phaseolus vulgaris SUT1.1 is a high affinity sucrose‐proton co‐transporter
Plant sucrose transporters are required for phloem loading, and therefore are essential for plant growth and development. In common beans (Phaseolus vulgaris) there are only two sucrose transporters functionally characterized. Through a previous RNA‐seq study, we identified a putative sucrose transp...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7453976/ https://www.ncbi.nlm.nih.gov/pubmed/32885136 http://dx.doi.org/10.1002/pld3.260 |
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author | Santiago, James P. Ward, John M. Sharkey, Thomas D. |
author_facet | Santiago, James P. Ward, John M. Sharkey, Thomas D. |
author_sort | Santiago, James P. |
collection | PubMed |
description | Plant sucrose transporters are required for phloem loading, and therefore are essential for plant growth and development. In common beans (Phaseolus vulgaris) there are only two sucrose transporters functionally characterized. Through a previous RNA‐seq study, we identified a putative sucrose transporter in common bean, which we hypothesize to function in import of sucrose into plant cells. In silico analysis revealed that PvSUT1.1 is a putative sucrose‐proton co‐transporter distinct from other characterized sucrose transporters in common bean indicating that this is a previously undescribed transporter protein in beans. Further analysis revealed that PvSUT1.1 shares high protein sequence homology to the phloem loader Arabidopsis SUC2; both have 12 transmembrane domains, a typical characteristic of plant sucrose transporters. Heterologous expression in yeast further showed PvSUT1.1 to be functional and it imported sucrose into yeast cells with a K(m) of 0.7 mM sucrose. Import of sucrose through PvSUT1.1 is also pH‐dependent with highest uptake at pH 4.0, and activity is lost in the presence of the uncoupler carbonyl cyanide 3‐chlorophenylhydrazone. Consistent with identification of PvSUT1.1 as a Type I transporter, PvSUT1.1 also transports esculin. Finally, PvSUT1.1 showed expression in multiple tissues and the protein was localized to the plasma membrane. The results show that PvSUT1.1 is a sucrose transporter that is probably involved in the uptake of sucrose into source and sink cells. The potential role of PvSUT1.1 in leaf phloem loading of sucrose in common beans and its importance in heat tolerance of reproductive tissues are further discussed. |
format | Online Article Text |
id | pubmed-7453976 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-74539762020-09-02 Phaseolus vulgaris SUT1.1 is a high affinity sucrose‐proton co‐transporter Santiago, James P. Ward, John M. Sharkey, Thomas D. Plant Direct Original Research Plant sucrose transporters are required for phloem loading, and therefore are essential for plant growth and development. In common beans (Phaseolus vulgaris) there are only two sucrose transporters functionally characterized. Through a previous RNA‐seq study, we identified a putative sucrose transporter in common bean, which we hypothesize to function in import of sucrose into plant cells. In silico analysis revealed that PvSUT1.1 is a putative sucrose‐proton co‐transporter distinct from other characterized sucrose transporters in common bean indicating that this is a previously undescribed transporter protein in beans. Further analysis revealed that PvSUT1.1 shares high protein sequence homology to the phloem loader Arabidopsis SUC2; both have 12 transmembrane domains, a typical characteristic of plant sucrose transporters. Heterologous expression in yeast further showed PvSUT1.1 to be functional and it imported sucrose into yeast cells with a K(m) of 0.7 mM sucrose. Import of sucrose through PvSUT1.1 is also pH‐dependent with highest uptake at pH 4.0, and activity is lost in the presence of the uncoupler carbonyl cyanide 3‐chlorophenylhydrazone. Consistent with identification of PvSUT1.1 as a Type I transporter, PvSUT1.1 also transports esculin. Finally, PvSUT1.1 showed expression in multiple tissues and the protein was localized to the plasma membrane. The results show that PvSUT1.1 is a sucrose transporter that is probably involved in the uptake of sucrose into source and sink cells. The potential role of PvSUT1.1 in leaf phloem loading of sucrose in common beans and its importance in heat tolerance of reproductive tissues are further discussed. John Wiley and Sons Inc. 2020-08-28 /pmc/articles/PMC7453976/ /pubmed/32885136 http://dx.doi.org/10.1002/pld3.260 Text en © 2020 The Authors. Plant Direct published by American Society of Plant Biologists and the Society for Experimental Biology and John Wiley & Sons Ltd This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes. |
spellingShingle | Original Research Santiago, James P. Ward, John M. Sharkey, Thomas D. Phaseolus vulgaris SUT1.1 is a high affinity sucrose‐proton co‐transporter |
title |
Phaseolus vulgaris SUT1.1 is a high affinity sucrose‐proton co‐transporter |
title_full |
Phaseolus vulgaris SUT1.1 is a high affinity sucrose‐proton co‐transporter |
title_fullStr |
Phaseolus vulgaris SUT1.1 is a high affinity sucrose‐proton co‐transporter |
title_full_unstemmed |
Phaseolus vulgaris SUT1.1 is a high affinity sucrose‐proton co‐transporter |
title_short |
Phaseolus vulgaris SUT1.1 is a high affinity sucrose‐proton co‐transporter |
title_sort | phaseolus vulgaris sut1.1 is a high affinity sucrose‐proton co‐transporter |
topic | Original Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7453976/ https://www.ncbi.nlm.nih.gov/pubmed/32885136 http://dx.doi.org/10.1002/pld3.260 |
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