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Plant aquaporins : their molecular biology, biophysics and significance for plant water relations

Identifieur interne : 006302 ( PascalFrancis/Corpus ); précédent : 006301; suivant : 006303

Plant 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. Smith

Source :

RBID : Pascal:99-0374894

Descripteurs français

English descriptors

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.

pA  
A01 01  1    @0 0022-0957
A02 01      @0 JEBOA6
A03   1    @0 J. Exp. Bot.
A05       @2 50
A06       @3 NS
A08 01  1  ENG  @1 Plant aquaporins : their molecular biology, biophysics and significance for plant water relations
A09 01  1  ENG  @1 Membrane transport: mechanisms, modulation and manipulation
A11 01  1    @1 TYERMAN (S. D.)
A11 02  1    @1 BOHNERT (H. J.)
A11 03  1    @1 MAUREL (C.)
A11 04  1    @1 STEUDLE (E.)
A11 05  1    @1 SMITH (J. A. C.)
A12 01  1    @1 HALL (John) @9 ed.
A12 02  1    @1 BLATT (Michael) @9 ed.
A12 03  1    @1 LEIGH (Roger) @9 ed.
A14 01      @1 School of Biological Sciences, Flinders University of South Australia, GPO Box 2100 @2 Adelaide, South Australia 5001 @3 AUS @Z 1 aut.
A14 02      @1 Departments of Biochemistry, Molecular and Cellular Biology, and Plant Sciences, University of Arizona @2 Tucson, Arizona 85721 @3 USA @Z 2 aut.
A14 03      @1 Institut des Sciences Végétales, CNRS, Avenue de la Terasse @2 91198 Gif-sur-Yvette @3 FRA @Z 3 aut.
A14 04      @1 Lehrstuhl für Pflanzenökologie, Universität Bayreuth, Universitätsstrasse 30 @2 95440 Bayreuth @3 DEU @Z 4 aut.
A14 05      @1 Department of Plant Sciences, University of Oxford, South Parks Road @2 Oxford OX1 3RB @3 GBR @Z 5 aut.
A20       @1 1055-1071
A21       @1 1999
A23 01      @0 ENG
A43 01      @1 INIST @2 6923 @5 354000085387880140
A44       @0 0000 @1 © 1999 INIST-CNRS. All rights reserved.
A45       @0 3 p.1/4
A47 01  1    @0 99-0374894
A60       @1 P @2 C
A61       @0 A
A64 01  1    @0 Journal of Experimental Botany
A66 01      @0 GBR
C01 01    ENG  @0 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.
C02 01  X    @0 002A10B03
C03 01  X  FRE  @0 Transport membranaire @5 01
C03 01  X  ENG  @0 Membrane transport @5 01
C03 01  X  SPA  @0 Transporte membranal @5 01
C03 02  X  FRE  @0 Eau @5 02
C03 02  X  ENG  @0 Water @5 02
C03 02  X  SPA  @0 Agua @5 02
C03 03  X  FRE  @0 Aquaporine @5 03
C03 03  X  ENG  @0 Aquaporin @5 03
C03 03  X  SPA  @0 Aquaporina @5 03
C03 04  X  FRE  @0 Végétal @5 04
C03 04  X  ENG  @0 Vegetals @5 04
C03 04  X  SPA  @0 Vegetal @5 04
C03 05  X  FRE  @0 Biophysique @5 05
C03 05  X  ENG  @0 Biophysics @5 05
C03 05  X  SPA  @0 Biofísica @5 05
C03 06  X  FRE  @0 Relation structure fonction @5 06
C03 06  X  ENG  @0 Structure function relationship @5 06
C03 06  X  SPA  @0 Relación estructura función @5 06
C03 07  X  FRE  @0 Conductivité hydraulique @5 07
C03 07  X  ENG  @0 Hydraulic conductivity @5 07
C03 07  X  SPA  @0 Conductividad hidráulica @5 07
C03 08  X  FRE  @0 Perméabilité cellulaire @5 08
C03 08  X  ENG  @0 Cell permeability @5 08
C03 08  X  SPA  @0 Permeabilidad celular @5 08
C03 09  X  FRE  @0 Cinétique @5 09
C03 09  X  ENG  @0 Kinetics @5 09
C03 09  X  SPA  @0 Cinética @5 09
C07 01  X  FRE  @0 Régime hydrique @5 33
C07 01  X  ENG  @0 Water regime @5 33
C07 01  X  SPA  @0 Régimen hídrico @5 33
N21       @1 242
pR  
A30 01  1  ENG  @1 International Workshop on Plant Membrane Biology @2 11 @3 Cambridge GBR @4 1998-08-09

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:99-0374894

Le document en format XML

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<fC03 i1="06" i2="X" l="FRE">
<s0>Relation structure fonction</s0>
<s5>06</s5>
</fC03>
<fC03 i1="06" i2="X" l="ENG">
<s0>Structure function relationship</s0>
<s5>06</s5>
</fC03>
<fC03 i1="06" i2="X" l="SPA">
<s0>Relación estructura función</s0>
<s5>06</s5>
</fC03>
<fC03 i1="07" i2="X" l="FRE">
<s0>Conductivité hydraulique</s0>
<s5>07</s5>
</fC03>
<fC03 i1="07" i2="X" l="ENG">
<s0>Hydraulic conductivity</s0>
<s5>07</s5>
</fC03>
<fC03 i1="07" i2="X" l="SPA">
<s0>Conductividad hidráulica</s0>
<s5>07</s5>
</fC03>
<fC03 i1="08" i2="X" l="FRE">
<s0>Perméabilité cellulaire</s0>
<s5>08</s5>
</fC03>
<fC03 i1="08" i2="X" l="ENG">
<s0>Cell permeability</s0>
<s5>08</s5>
</fC03>
<fC03 i1="08" i2="X" l="SPA">
<s0>Permeabilidad celular</s0>
<s5>08</s5>
</fC03>
<fC03 i1="09" i2="X" l="FRE">
<s0>Cinétique</s0>
<s5>09</s5>
</fC03>
<fC03 i1="09" i2="X" l="ENG">
<s0>Kinetics</s0>
<s5>09</s5>
</fC03>
<fC03 i1="09" i2="X" l="SPA">
<s0>Cinética</s0>
<s5>09</s5>
</fC03>
<fC07 i1="01" i2="X" l="FRE">
<s0>Régime hydrique</s0>
<s5>33</s5>
</fC07>
<fC07 i1="01" i2="X" l="ENG">
<s0>Water regime</s0>
<s5>33</s5>
</fC07>
<fC07 i1="01" i2="X" l="SPA">
<s0>Régimen hídrico</s0>
<s5>33</s5>
</fC07>
<fN21>
<s1>242</s1>
</fN21>
</pA>
<pR>
<fA30 i1="01" i2="1" l="ENG">
<s1>International Workshop on Plant Membrane Biology</s1>
<s2>11</s2>
<s3>Cambridge GBR</s3>
<s4>1998-08-09</s4>
</fA30>
</pR>
</standard>
<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>
<LO>INIST-6923.354000085387880140</LO>
<ID>99-0374894</ID>
</server>
</inist>
</record>

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