Plant aquaporins : their molecular biology, biophysics and significance for plant water relations
Identifieur interne : 006302 ( PascalFrancis/Corpus ); précédent : 006301; suivant : 006303Plant aquaporins : their molecular biology, biophysics and significance for plant water relations
Auteurs : S. D. Tyerman ; H. J. Bohnert ; C. Maurel ; E. Steudle ; J. A. C. SmithSource :
- Journal of Experimental Botany [ 0022-0957 ] ; 1999.
Descripteurs français
- Pascal (Inist)
English descriptors
- KwdEn :
Abstract
Over the last decade, considerable advances have occurred in understanding the molecular biology and biophysics of water permeation across plant membranes and tissues. Spurred on by the rapid advances in cloning and functional characterization of a super-family of major intrinsic proteins, some of which function as aquaporins, the biophysics of transport of water and small non-electrolytes across plant membranes is being re-examined based on the proposed function of these membrane-integral proteins in their native membranes. This review focuses on a number of issues that are central to an understanding of aquaporin function: (1) the need to be able to test for water-channel activity in native membranes; (2) the implications of the observed solute/water selectivity of aquaporins; (3) the putative functional roles of aquaporins at the cell, tissue and organ levels in plants; and (4) information that can be obtained from studies of the abundance, diversity and expression patterns of aquaporins. It is clear that to answer many of the critical questions that remain concerning aquaporin function, combined studies using appropriate molecular and biophysical techniques will be required.
Notice en format standard (ISO 2709)
Pour connaître la documentation sur le format Inist Standard.
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Format Inist (serveur)
NO : | PASCAL 99-0374894 INIST |
---|---|
ET : | Plant aquaporins : their molecular biology, biophysics and significance for plant water relations |
AU : | TYERMAN (S. D.); BOHNERT (H. J.); MAUREL (C.); STEUDLE (E.); SMITH (J. A. C.); HALL (John); BLATT (Michael); LEIGH (Roger) |
AF : | School of Biological Sciences, Flinders University of South Australia, GPO Box 2100/Adelaide, South Australia 5001/Australie (1 aut.); Departments of Biochemistry, Molecular and Cellular Biology, and Plant Sciences, University of Arizona/Tucson, Arizona 85721/Etats-Unis (2 aut.); Institut des Sciences Végétales, CNRS, Avenue de la Terasse/91198 Gif-sur-Yvette/France (3 aut.); Lehrstuhl für Pflanzenökologie, Universität Bayreuth, Universitätsstrasse 30/95440 Bayreuth/Allemagne (4 aut.); Department of Plant Sciences, University of Oxford, South Parks Road/Oxford OX1 3RB/Royaume-Uni (5 aut.) |
DT : | Publication en série; Congrès; Niveau analytique |
SO : | Journal of Experimental Botany; ISSN 0022-0957; Coden JEBOA6; Royaume-Uni; Da. 1999; Vol. 50; No. NS; Pp. 1055-1071; Bibl. 3 p.1/4 |
LA : | Anglais |
EA : | Over the last decade, considerable advances have occurred in understanding the molecular biology and biophysics of water permeation across plant membranes and tissues. Spurred on by the rapid advances in cloning and functional characterization of a super-family of major intrinsic proteins, some of which function as aquaporins, the biophysics of transport of water and small non-electrolytes across plant membranes is being re-examined based on the proposed function of these membrane-integral proteins in their native membranes. This review focuses on a number of issues that are central to an understanding of aquaporin function: (1) the need to be able to test for water-channel activity in native membranes; (2) the implications of the observed solute/water selectivity of aquaporins; (3) the putative functional roles of aquaporins at the cell, tissue and organ levels in plants; and (4) information that can be obtained from studies of the abundance, diversity and expression patterns of aquaporins. It is clear that to answer many of the critical questions that remain concerning aquaporin function, combined studies using appropriate molecular and biophysical techniques will be required. |
CC : | 002A10B03 |
FD : | Transport membranaire; Eau; Aquaporine; Végétal; Biophysique; Relation structure fonction; Conductivité hydraulique; Perméabilité cellulaire; Cinétique |
FG : | Régime hydrique |
ED : | Membrane transport; Water; Aquaporin; Vegetals; Biophysics; Structure function relationship; Hydraulic conductivity; Cell permeability; Kinetics |
EG : | Water regime |
SD : | Transporte membranal; Agua; Aquaporina; Vegetal; Biofísica; Relación estructura función; Conductividad hidráulica; Permeabilidad celular; Cinética |
LO : | INIST-6923.354000085387880140 |
ID : | 99-0374894 |
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Pascal:99-0374894Le document en format XML
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<front><div type="abstract" xml:lang="en">Over the last decade, considerable advances have occurred in understanding the molecular biology and biophysics of water permeation across plant membranes and tissues. Spurred on by the rapid advances in cloning and functional characterization of a super-family of major intrinsic proteins, some of which function as aquaporins, the biophysics of transport of water and small non-electrolytes across plant membranes is being re-examined based on the proposed function of these membrane-integral proteins in their native membranes. This review focuses on a number of issues that are central to an understanding of aquaporin function: (1) the need to be able to test for water-channel activity in native membranes; (2) the implications of the observed solute/water selectivity of aquaporins; (3) the putative functional roles of aquaporins at the cell, tissue and organ levels in plants; and (4) information that can be obtained from studies of the abundance, diversity and expression patterns of aquaporins. It is clear that to answer many of the critical questions that remain concerning aquaporin function, combined studies using appropriate molecular and biophysical techniques will be required.</div>
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<server><NO>PASCAL 99-0374894 INIST</NO>
<ET>Plant aquaporins : their molecular biology, biophysics and significance for plant water relations</ET>
<AU>TYERMAN (S. D.); BOHNERT (H. J.); MAUREL (C.); STEUDLE (E.); SMITH (J. A. C.); HALL (John); BLATT (Michael); LEIGH (Roger)</AU>
<AF>School of Biological Sciences, Flinders University of South Australia, GPO Box 2100/Adelaide, South Australia 5001/Australie (1 aut.); Departments of Biochemistry, Molecular and Cellular Biology, and Plant Sciences, University of Arizona/Tucson, Arizona 85721/Etats-Unis (2 aut.); Institut des Sciences Végétales, CNRS, Avenue de la Terasse/91198 Gif-sur-Yvette/France (3 aut.); Lehrstuhl für Pflanzenökologie, Universität Bayreuth, Universitätsstrasse 30/95440 Bayreuth/Allemagne (4 aut.); Department of Plant Sciences, University of Oxford, South Parks Road/Oxford OX1 3RB/Royaume-Uni (5 aut.)</AF>
<DT>Publication en série; Congrès; Niveau analytique</DT>
<SO>Journal of Experimental Botany; ISSN 0022-0957; Coden JEBOA6; Royaume-Uni; Da. 1999; Vol. 50; No. NS; Pp. 1055-1071; Bibl. 3 p.1/4</SO>
<LA>Anglais</LA>
<EA>Over the last decade, considerable advances have occurred in understanding the molecular biology and biophysics of water permeation across plant membranes and tissues. Spurred on by the rapid advances in cloning and functional characterization of a super-family of major intrinsic proteins, some of which function as aquaporins, the biophysics of transport of water and small non-electrolytes across plant membranes is being re-examined based on the proposed function of these membrane-integral proteins in their native membranes. This review focuses on a number of issues that are central to an understanding of aquaporin function: (1) the need to be able to test for water-channel activity in native membranes; (2) the implications of the observed solute/water selectivity of aquaporins; (3) the putative functional roles of aquaporins at the cell, tissue and organ levels in plants; and (4) information that can be obtained from studies of the abundance, diversity and expression patterns of aquaporins. It is clear that to answer many of the critical questions that remain concerning aquaporin function, combined studies using appropriate molecular and biophysical techniques will be required.</EA>
<CC>002A10B03</CC>
<FD>Transport membranaire; Eau; Aquaporine; Végétal; Biophysique; Relation structure fonction; Conductivité hydraulique; Perméabilité cellulaire; Cinétique</FD>
<FG>Régime hydrique</FG>
<ED>Membrane transport; Water; Aquaporin; Vegetals; Biophysics; Structure function relationship; Hydraulic conductivity; Cell permeability; Kinetics</ED>
<EG>Water regime</EG>
<SD>Transporte membranal; Agua; Aquaporina; Vegetal; Biofísica; Relación estructura función; Conductividad hidráulica; Permeabilidad celular; Cinética</SD>
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<ID>99-0374894</ID>
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