Point mutations in the barley HvHAK1 potassium transporter lead to improved K+-nutrition and enhanced resistance to salt stress
Members of group I KT-HAK-KUP transporters play an important role in K+ acquisition by plant roots, a process that is strongly affected by salt stress. A PCR-based random mutagenesis approach on HvHAK1 allowed identification of V366I and R591C substitutions, which confer enhanced K+-capture, and imp...
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Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00145793_v582_n28_p3922_Mangano http://hdl.handle.net/20.500.12110/paper_00145793_v582_n28_p3922_Mangano |
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paper:paper_00145793_v582_n28_p3922_Mangano2023-06-08T14:37:43Z Point mutations in the barley HvHAK1 potassium transporter lead to improved K+-nutrition and enhanced resistance to salt stress Silberstein Cuña, Susana Iris Santa María, Guillermo Esteban HAK KUP Potassium Sodium Transporter ammonium chloride lithium chloride sodium chloride amino acid substitution article barley mutagenesis nonhuman nutrition point mutation polymerase chain reaction potassium transport priority journal protein domain salt stress yeast cell Amino Acid Substitution Arginine Cation Transport Proteins Cysteine Ion Transport Isoleucine Osmotic Pressure Plant Proteins Point Mutation Potassium Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Salinity Sodium Sodium Chloride Valine Hordeum Members of group I KT-HAK-KUP transporters play an important role in K+ acquisition by plant roots, a process that is strongly affected by salt stress. A PCR-based random mutagenesis approach on HvHAK1 allowed identification of V366I and R591C substitutions, which confer enhanced K+-capture, and improved NaCl, LiCl and NH4Cl tolerance, to yeast cells. Improved K+-capture was linked to an enhanced Vmax. Results reveal an intrinsic protective effect of K+, and assign an important role to the 8th transmembrane domain, as well as the C-terminus, in determining the maximum capacity for the transport of K+ in KT-HAK-KUP transporters. © 2008 Federation of European Biochemical Societies. Fil:Silberstein, S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Santa-María, G.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2008 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00145793_v582_n28_p3922_Mangano http://hdl.handle.net/20.500.12110/paper_00145793_v582_n28_p3922_Mangano |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
HAK KUP Potassium Sodium Transporter ammonium chloride lithium chloride sodium chloride amino acid substitution article barley mutagenesis nonhuman nutrition point mutation polymerase chain reaction potassium transport priority journal protein domain salt stress yeast cell Amino Acid Substitution Arginine Cation Transport Proteins Cysteine Ion Transport Isoleucine Osmotic Pressure Plant Proteins Point Mutation Potassium Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Salinity Sodium Sodium Chloride Valine Hordeum |
spellingShingle |
HAK KUP Potassium Sodium Transporter ammonium chloride lithium chloride sodium chloride amino acid substitution article barley mutagenesis nonhuman nutrition point mutation polymerase chain reaction potassium transport priority journal protein domain salt stress yeast cell Amino Acid Substitution Arginine Cation Transport Proteins Cysteine Ion Transport Isoleucine Osmotic Pressure Plant Proteins Point Mutation Potassium Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Salinity Sodium Sodium Chloride Valine Hordeum Silberstein Cuña, Susana Iris Santa María, Guillermo Esteban Point mutations in the barley HvHAK1 potassium transporter lead to improved K+-nutrition and enhanced resistance to salt stress |
topic_facet |
HAK KUP Potassium Sodium Transporter ammonium chloride lithium chloride sodium chloride amino acid substitution article barley mutagenesis nonhuman nutrition point mutation polymerase chain reaction potassium transport priority journal protein domain salt stress yeast cell Amino Acid Substitution Arginine Cation Transport Proteins Cysteine Ion Transport Isoleucine Osmotic Pressure Plant Proteins Point Mutation Potassium Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Salinity Sodium Sodium Chloride Valine Hordeum |
description |
Members of group I KT-HAK-KUP transporters play an important role in K+ acquisition by plant roots, a process that is strongly affected by salt stress. A PCR-based random mutagenesis approach on HvHAK1 allowed identification of V366I and R591C substitutions, which confer enhanced K+-capture, and improved NaCl, LiCl and NH4Cl tolerance, to yeast cells. Improved K+-capture was linked to an enhanced Vmax. Results reveal an intrinsic protective effect of K+, and assign an important role to the 8th transmembrane domain, as well as the C-terminus, in determining the maximum capacity for the transport of K+ in KT-HAK-KUP transporters. © 2008 Federation of European Biochemical Societies. |
author |
Silberstein Cuña, Susana Iris Santa María, Guillermo Esteban |
author_facet |
Silberstein Cuña, Susana Iris Santa María, Guillermo Esteban |
author_sort |
Silberstein Cuña, Susana Iris |
title |
Point mutations in the barley HvHAK1 potassium transporter lead to improved K+-nutrition and enhanced resistance to salt stress |
title_short |
Point mutations in the barley HvHAK1 potassium transporter lead to improved K+-nutrition and enhanced resistance to salt stress |
title_full |
Point mutations in the barley HvHAK1 potassium transporter lead to improved K+-nutrition and enhanced resistance to salt stress |
title_fullStr |
Point mutations in the barley HvHAK1 potassium transporter lead to improved K+-nutrition and enhanced resistance to salt stress |
title_full_unstemmed |
Point mutations in the barley HvHAK1 potassium transporter lead to improved K+-nutrition and enhanced resistance to salt stress |
title_sort |
point mutations in the barley hvhak1 potassium transporter lead to improved k+-nutrition and enhanced resistance to salt stress |
publishDate |
2008 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00145793_v582_n28_p3922_Mangano http://hdl.handle.net/20.500.12110/paper_00145793_v582_n28_p3922_Mangano |
work_keys_str_mv |
AT silbersteincunasusanairis pointmutationsinthebarleyhvhak1potassiumtransporterleadtoimprovedknutritionandenhancedresistancetosaltstress AT santamariaguillermoesteban pointmutationsinthebarleyhvhak1potassiumtransporterleadtoimprovedknutritionandenhancedresistancetosaltstress |
_version_ |
1768542920356397056 |