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OsMTP11 is localised at the Golgi and contributes to Mn tolerance
Membrane transporters play a key role in obtaining sufficient quantities of manganese (Mn) but also in protecting against Mn toxicity. We have characterized OsMTP11, a member of the Cation Diffusion Facilitator/Metal Tolerance Protein (CDF/MTP) family of metal cation transporters in Oryza sativa. We...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Nature Publishing Group UK
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5681648/ https://www.ncbi.nlm.nih.gov/pubmed/29127328 http://dx.doi.org/10.1038/s41598-017-15324-6 |
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author | Farthing, Emily C. Menguer, Paloma K. Fett, Janette Palma Williams, Lorraine E. |
author_facet | Farthing, Emily C. Menguer, Paloma K. Fett, Janette Palma Williams, Lorraine E. |
author_sort | Farthing, Emily C. |
collection | PubMed |
description | Membrane transporters play a key role in obtaining sufficient quantities of manganese (Mn) but also in protecting against Mn toxicity. We have characterized OsMTP11, a member of the Cation Diffusion Facilitator/Metal Tolerance Protein (CDF/MTP) family of metal cation transporters in Oryza sativa. We demonstrate that OsMTP11 functions in alleviating Mn toxicity as its expression can rescue the Mn-sensitive phenotype of the Arabidopsis mtp11-3 knockout mutant. When expressed stably in Arabidopsis and transiently in rice and tobacco, it localises to the Golgi. OsMTP11 partially rescues the Mn-hypersensitivity of the pmr1 yeast mutant but only slightly alleviates the Zn sensitivity of the zrc1 cot1 yeast mutant. Overall, these results suggest that OsMTP11 predominantly functions as a Mn-transporting CDF with lower affinity for Zn. Site-directed mutagenesis studies revealed four substitutions in OsMTP11 that appear to alter its transport activity. OsMTP11 harbouring a substitution of leucine 150 to a serine fully rescued pmr1 Mn-sensitivity at all concentrations tested. The other substitutions, including those at conserved DxxxD domains, reduced complementation of pmr1 to different levels. This indicates their importance for OsMTP11 function and is a starting point for refining transporter activity/specificity. |
format | Online Article Text |
id | pubmed-5681648 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-56816482017-11-17 OsMTP11 is localised at the Golgi and contributes to Mn tolerance Farthing, Emily C. Menguer, Paloma K. Fett, Janette Palma Williams, Lorraine E. Sci Rep Article Membrane transporters play a key role in obtaining sufficient quantities of manganese (Mn) but also in protecting against Mn toxicity. We have characterized OsMTP11, a member of the Cation Diffusion Facilitator/Metal Tolerance Protein (CDF/MTP) family of metal cation transporters in Oryza sativa. We demonstrate that OsMTP11 functions in alleviating Mn toxicity as its expression can rescue the Mn-sensitive phenotype of the Arabidopsis mtp11-3 knockout mutant. When expressed stably in Arabidopsis and transiently in rice and tobacco, it localises to the Golgi. OsMTP11 partially rescues the Mn-hypersensitivity of the pmr1 yeast mutant but only slightly alleviates the Zn sensitivity of the zrc1 cot1 yeast mutant. Overall, these results suggest that OsMTP11 predominantly functions as a Mn-transporting CDF with lower affinity for Zn. Site-directed mutagenesis studies revealed four substitutions in OsMTP11 that appear to alter its transport activity. OsMTP11 harbouring a substitution of leucine 150 to a serine fully rescued pmr1 Mn-sensitivity at all concentrations tested. The other substitutions, including those at conserved DxxxD domains, reduced complementation of pmr1 to different levels. This indicates their importance for OsMTP11 function and is a starting point for refining transporter activity/specificity. Nature Publishing Group UK 2017-11-10 /pmc/articles/PMC5681648/ /pubmed/29127328 http://dx.doi.org/10.1038/s41598-017-15324-6 Text en © The Author(s) 2017 Open Access This 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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Farthing, Emily C. Menguer, Paloma K. Fett, Janette Palma Williams, Lorraine E. OsMTP11 is localised at the Golgi and contributes to Mn tolerance |
title | OsMTP11 is localised at the Golgi and contributes to Mn tolerance |
title_full | OsMTP11 is localised at the Golgi and contributes to Mn tolerance |
title_fullStr | OsMTP11 is localised at the Golgi and contributes to Mn tolerance |
title_full_unstemmed | OsMTP11 is localised at the Golgi and contributes to Mn tolerance |
title_short | OsMTP11 is localised at the Golgi and contributes to Mn tolerance |
title_sort | osmtp11 is localised at the golgi and contributes to mn tolerance |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5681648/ https://www.ncbi.nlm.nih.gov/pubmed/29127328 http://dx.doi.org/10.1038/s41598-017-15324-6 |
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