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: Silberstein Cuña, Susana Iris, Santa María, Guillermo Esteban
Publicado: 2008
Materias:
HAK
KUP
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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spelling 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
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