OsMTP11 is localised at the Golgi and contributes to Mn tolerance

Detalhes bibliográficos
Autor(a) principal: Farthing, Emily
Data de Publicação: 2017
Outros Autores: Menguer, Paloma Koprovski, Fett, Janette Palma, Williams, Lorraine E.
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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spelling 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
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dc.identifier.issn.pt_BR.fl_str_mv 2045-2322
dc.identifier.nrb.pt_BR.fl_str_mv 001055118
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dc.relation.ispartof.pt_BR.fl_str_mv Scientific reports. London. Vol. 7, (Nov. 2017), article 15258, p. 1-13
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