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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Autores principales:	Mangano, S., Silberstein, S., Santa-María, G.E.
Formato:	JOUR
Materias:	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 Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Salinity Sodium Chloride Valine Hordeum
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_00145793_v582_n28_p3922_Mangano
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	todo:paper_00145793_v582_n28_p3922_Mangano
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spelling	todo:paper_00145793_v582_n28_p3922_Mangano2023-10-03T14:13:10Z Point mutations in the barley HvHAK1 potassium transporter lead to improved K+-nutrition and enhanced resistance to salt stress Mangano, S. Silberstein, S. Santa-María, G.E. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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 Mangano, S. Silberstein, S. Santa-María, G.E. 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.
format	JOUR
author	Mangano, S. Silberstein, S. Santa-María, G.E.
author_facet	Mangano, S. Silberstein, S. Santa-María, G.E.
author_sort	Mangano, S.
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
url	http://hdl.handle.net/20.500.12110/paper_00145793_v582_n28_p3922_Mangano
work_keys_str_mv	AT manganos pointmutationsinthebarleyhvhak1potassiumtransporterleadtoimprovedknutritionandenhancedresistancetosaltstress AT silbersteins pointmutationsinthebarleyhvhak1potassiumtransporterleadtoimprovedknutritionandenhancedresistancetosaltstress AT santamariage pointmutationsinthebarleyhvhak1potassiumtransporterleadtoimprovedknutritionandenhancedresistancetosaltstress
_version_	1807322388329660416

Point mutations in the barley HvHAK1 potassium transporter lead to improved K+-nutrition and enhanced resistance to salt stress

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