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HvALMT1 from barley is involved in the transport of organic anions
Members of the ALMT gene family contribute to the Al(3+) resistance of several plant species by facilitating malate efflux from root cells. The first member of this family to be cloned and characterized, TaALMT1, is responsible for most of the natural variation of Al(3+) resistance in wheat. The cur...
Autores principales: | , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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Oxford University Press
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2837267/ https://www.ncbi.nlm.nih.gov/pubmed/20176888 http://dx.doi.org/10.1093/jxb/erq023 |
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author | Gruber, Benjamin D. Ryan, Peter R. Richardson, Alan E. Tyerman, Stephen D. Ramesh, Sunita Hebb, Diane M. Howitt, Susan M. Delhaize, Emmanuel |
author_facet | Gruber, Benjamin D. Ryan, Peter R. Richardson, Alan E. Tyerman, Stephen D. Ramesh, Sunita Hebb, Diane M. Howitt, Susan M. Delhaize, Emmanuel |
author_sort | Gruber, Benjamin D. |
collection | PubMed |
description | Members of the ALMT gene family contribute to the Al(3+) resistance of several plant species by facilitating malate efflux from root cells. The first member of this family to be cloned and characterized, TaALMT1, is responsible for most of the natural variation of Al(3+) resistance in wheat. The current study describes the isolation and characterization of HvALMT1, the barley gene with the greatest sequence similarity to TaALMT1. HvALMT1 is located on chromosome 2H which has not been associated with Al(3+) resistance in barley. The relatively low levels of HvALMT1 expression detected in root and shoot tissues were independent of external aluminium or phosphorus supply. Transgenic barley plants transformed with the HvALMT1 promoter fused to the green fluorescent protein (GFP) indicated that expression of HvALMT1 was relatively high in stomatal guard cells and in root tissues containing expanding cells. GFP fused to the C-terminus of the full HvALMT1 protein localized to the plasma membrane and motile vesicles within the cytoplasm. HvALMT1 conferred both inward and outward currents when expressed in Xenopus laevis oocytes that were bathed in a range of anions including malate. Both malate uptake and efflux were confirmed in oocyte assays using [(14)C]malate as a radiotracer. It is suggested that HvALMT1 functions as an anion channel to facilitate organic anion transport in stomatal function and expanding cells. |
format | Text |
id | pubmed-2837267 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-28372672010-03-15 HvALMT1 from barley is involved in the transport of organic anions Gruber, Benjamin D. Ryan, Peter R. Richardson, Alan E. Tyerman, Stephen D. Ramesh, Sunita Hebb, Diane M. Howitt, Susan M. Delhaize, Emmanuel J Exp Bot Research Papers Members of the ALMT gene family contribute to the Al(3+) resistance of several plant species by facilitating malate efflux from root cells. The first member of this family to be cloned and characterized, TaALMT1, is responsible for most of the natural variation of Al(3+) resistance in wheat. The current study describes the isolation and characterization of HvALMT1, the barley gene with the greatest sequence similarity to TaALMT1. HvALMT1 is located on chromosome 2H which has not been associated with Al(3+) resistance in barley. The relatively low levels of HvALMT1 expression detected in root and shoot tissues were independent of external aluminium or phosphorus supply. Transgenic barley plants transformed with the HvALMT1 promoter fused to the green fluorescent protein (GFP) indicated that expression of HvALMT1 was relatively high in stomatal guard cells and in root tissues containing expanding cells. GFP fused to the C-terminus of the full HvALMT1 protein localized to the plasma membrane and motile vesicles within the cytoplasm. HvALMT1 conferred both inward and outward currents when expressed in Xenopus laevis oocytes that were bathed in a range of anions including malate. Both malate uptake and efflux were confirmed in oocyte assays using [(14)C]malate as a radiotracer. It is suggested that HvALMT1 functions as an anion channel to facilitate organic anion transport in stomatal function and expanding cells. Oxford University Press 2010-03 2010-02-22 /pmc/articles/PMC2837267/ /pubmed/20176888 http://dx.doi.org/10.1093/jxb/erq023 Text en © 2010 The Author(s). This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. This paper is available online free of all access charges (see http://jxb.oxfordjournals.org/open_access.html for further details) |
spellingShingle | Research Papers Gruber, Benjamin D. Ryan, Peter R. Richardson, Alan E. Tyerman, Stephen D. Ramesh, Sunita Hebb, Diane M. Howitt, Susan M. Delhaize, Emmanuel HvALMT1 from barley is involved in the transport of organic anions |
title | HvALMT1 from barley is involved in the transport of organic anions |
title_full | HvALMT1 from barley is involved in the transport of organic anions |
title_fullStr | HvALMT1 from barley is involved in the transport of organic anions |
title_full_unstemmed | HvALMT1 from barley is involved in the transport of organic anions |
title_short | HvALMT1 from barley is involved in the transport of organic anions |
title_sort | hvalmt1 from barley is involved in the transport of organic anions |
topic | Research Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2837267/ https://www.ncbi.nlm.nih.gov/pubmed/20176888 http://dx.doi.org/10.1093/jxb/erq023 |
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