OsMTP11 is localised at the Golgi and contributes to Mn tolerance
Autor(a) principal: | |
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Data de Publicação: | 2017 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UFRGS |
Texto Completo: | http://hdl.handle.net/10183/225527 |
Resumo: | 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. |
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Farthing, EmilyMenguer, Paloma KoprovskiFett, Janette PalmaWilliams, Lorraine E.2021-08-11T04:47:40Z20172045-2322http://hdl.handle.net/10183/225527001055118Membrane 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.application/pdfengScientific reports. London. Vol. 7, (Nov. 2017), article 15258, p. 1-13Oryza sativaArabidopsisOsMTP11 is localised at the Golgi and contributes to Mn toleranceEstrangeiroinfo:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UFRGSinstname:Universidade Federal do Rio Grande do Sul (UFRGS)instacron:UFRGSTEXT001055118.pdf.txt001055118.pdf.txtExtracted Texttext/plain59850http://www.lume.ufrgs.br/bitstream/10183/225527/2/001055118.pdf.txtf77ebfbd5adc31c11429142652280843MD52ORIGINAL001055118.pdfTexto completo (inglês)application/pdf5680439http://www.lume.ufrgs.br/bitstream/10183/225527/1/001055118.pdfaf46dd5d618bef9ab71ccc210fa8cc89MD5110183/2255272023-05-05 03:20:17.023359oai:www.lume.ufrgs.br:10183/225527Repositório de PublicaçõesPUBhttps://lume.ufrgs.br/oai/requestopendoar:2023-05-05T06:20:17Repositório Institucional da UFRGS - Universidade Federal do Rio Grande do Sul (UFRGS)false |
dc.title.pt_BR.fl_str_mv |
OsMTP11 is localised at the Golgi and contributes to Mn tolerance |
title |
OsMTP11 is localised at the Golgi and contributes to Mn tolerance |
spellingShingle |
OsMTP11 is localised at the Golgi and contributes to Mn tolerance Farthing, Emily Oryza sativa Arabidopsis |
title_short |
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_sort |
OsMTP11 is localised at the Golgi and contributes to Mn tolerance |
author |
Farthing, Emily |
author_facet |
Farthing, Emily Menguer, Paloma Koprovski Fett, Janette Palma Williams, Lorraine E. |
author_role |
author |
author2 |
Menguer, Paloma Koprovski Fett, Janette Palma Williams, Lorraine E. |
author2_role |
author author author |
dc.contributor.author.fl_str_mv |
Farthing, Emily Menguer, Paloma Koprovski Fett, Janette Palma Williams, Lorraine E. |
dc.subject.por.fl_str_mv |
Oryza sativa Arabidopsis |
topic |
Oryza sativa Arabidopsis |
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. |
publishDate |
2017 |
dc.date.issued.fl_str_mv |
2017 |
dc.date.accessioned.fl_str_mv |
2021-08-11T04:47:40Z |
dc.type.driver.fl_str_mv |
Estrangeiro info:eu-repo/semantics/article |
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info:eu-repo/semantics/publishedVersion |
format |
article |
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publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10183/225527 |
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2045-2322 |
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001055118 |
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2045-2322 001055118 |
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http://hdl.handle.net/10183/225527 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartof.pt_BR.fl_str_mv |
Scientific reports. London. Vol. 7, (Nov. 2017), article 15258, p. 1-13 |
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info:eu-repo/semantics/openAccess |
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openAccess |
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application/pdf |
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