AustralieFrV1, PascalFrancis, Corpus, bibRecord, 001D31

Characterization of a transport activity for long-chain peptides in barley mesophyll vacuoles

Identifieur interne : 001D31 ( PascalFrancis/Corpus ); précédent : 001D30; suivant : 001D32

Characterization of a transport activity for long-chain peptides in barley mesophyll vacuoles

Auteurs : Magali Schnell Ramos ; Rupert Abele ; Reka Nagy ; Marianne Suter Grotemeyer ; Robert Tampe ; Doris Rentsch ; Enrico Martinoia

Source :

Journal of experimental botany [ 0022-0957 ] ; 2011.

RBID : Pascal:11-0251115

Descripteurs français

Pascal (Inist)
- Transport, Peptide, Orge, Feuille végétal, Vacuole, Botanique, Hordeum vulgare, Chaîne longue, Transporteur ABC, Mésophylle.

English descriptors

KwdEn :
- ABC transporter, Barley, Botany, Hordeum vulgare, Long chain, Mesophyll, Peptides, Plant leaf, Transport, Vacuole.

Abstract

The plant vacuole is the largest compartment in a fully expanded plant cell. While only very limited metabolic activity can be observed within the vacuole, the majority of the hydrolytic activities, including proteolytic activities reside in this organelle. Since it is assumed that protein degradation by the proteasome results in the production of peptides with a size of 3-30 amino acids, we were interested to show whether the tonoplast exhibits a transport activity, which could deliver these peptides into the vacuole for final degradation. It is shown here that isolated barley mesophyll vacuoles take up peptides of 9-27 amino acids in a strictly ATP-dependent manner. Uptake is inhibited by vanadate, but not by NH⁺₄, while GTP could partially substitute for ATP. The apparent affinity for the 9 amino acid peptide was 15 μM, suggesting that peptides are efficiently transferred to the vacuole in vivo. Inhibition experiments showed that peptides with a chain length below 10 amino acids did not compete as efficiently as longer peptides for the uptake of the 9 amino acid peptide. Our results suggest that vacuoles contain at least one peptide transporter that belongs to the ABC-type transporters, which efficiently exports long-chain peptides from the cytosol into the vacuole for final degradation.

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

A01	`01`	`1`		`@0 0022-0957`
A02	`01`			`@0 JEBOA6`
A03		`1`		`@0 J. exp. bot.`
A05				`@2 62`
A06				`@2 7`
A08	`01`	`1`	`ENG`	`@1 Characterization of a transport activity for long-chain peptides in barley mesophyll vacuoles`
A09	`01`	`1`	`ENG`	`@1 PLANT MEMBRANE BIOLOGY`
A11	`01`	`1`		`@1 SCHNELL RAMOS (Magali)`
A11	`02`	`1`		`@1 ABELE (Rupert)`
A11	`03`	`1`		`@1 NAGY (Reka)`
A11	`04`	`1`		`@1 SUTER GROTEMEYER (Marianne)`
A11	`05`	`1`		`@1 TAMPE (Robert)`
A11	`06`	`1`		`@1 RENTSCH (Doris)`
A11	`07`	`1`		`@1 MARTINOIA (Enrico)`
A12	`01`	`1`		`@1 GILLIHAM (M.) @9 limin.`
A14	`01`			`@1 Institute of Plant Biology, University Zurich, Zollikerstrasse 107 @2 8008 Zurich @3 CHE @Z 1 aut. @Z 3 aut. @Z 7 aut.`
A14	`02`			`@1 Institute of Biochemistry, Biocenter, Goethe-University Frankfurt, Max-von-Laue Strasse 9 9 @2 60438 Frankfurt am Main @3 DEU @Z 2 aut. @Z 5 aut.`
A14	`03`			`@1 Institute of Plant Sciences, University of Bern, Altenbergrain 21 @2 3013 Bern @3 CHE @Z 4 aut. @Z 6 aut.`
A14	`04`			`@1 Institut des Sciences du Végétal, CNRS, 1, av. de la Terrasse @2 91198 Gif-sur-Yvette @3 FRA @Z 1 aut.`
A15	`01`			`@1 School of Agriculture, Food and Wine & Waite Research Institute, University of Adelaide @3 AUS @Z 1 aut.`
A20				`@1 2403-2410`
A21				`@1 2011`
A23	`01`			`@0 ENG`
A43	`01`			`@1 INIST @2 6923 @5 354000191483460140`
A44				`@0 0000 @1 © 2011 INIST-CNRS. All rights reserved.`
A45				`@0 1 p.`
A47	`01`	`1`		`@0 11-0251115`
A60				`@1 P @3 PR`
A61				`@0 A`
A64	`01`	`1`		`@0 Journal of experimental botany`
A66	`01`			`@0 GBR`
C01	`01`		`ENG`	@0 The plant vacuole is the largest compartment in a fully expanded plant cell. While only very limited metabolic activity can be observed within the vacuole, the majority of the hydrolytic activities, including proteolytic activities reside in this organelle. Since it is assumed that protein degradation by the proteasome results in the production of peptides with a size of 3-30 amino acids, we were interested to show whether the tonoplast exhibits a transport activity, which could deliver these peptides into the vacuole for final degradation. It is shown here that isolated barley mesophyll vacuoles take up peptides of 9-27 amino acids in a strictly ATP-dependent manner. Uptake is inhibited by vanadate, but not by NH⁺₄, while GTP could partially substitute for ATP. The apparent affinity for the 9 amino acid peptide was 15 μM, suggesting that peptides are efficiently transferred to the vacuole in vivo. Inhibition experiments showed that peptides with a chain length below 10 amino acids did not compete as efficiently as longer peptides for the uptake of the 9 amino acid peptide. Our results suggest that vacuoles contain at least one peptide transporter that belongs to the ABC-type transporters, which efficiently exports long-chain peptides from the cytosol into the vacuole for final degradation.
C02	`01`	`X`		`@0 002A10`
C03	`01`	`X`	`FRE`	`@0 Transport @5 01`
C03	`01`	`X`	`ENG`	`@0 Transport @5 01`
C03	`01`	`X`	`SPA`	`@0 Transporte @5 01`
C03	`02`	`X`	`FRE`	`@0 Peptide @5 02`
C03	`02`	`X`	`ENG`	`@0 Peptides @5 02`
C03	`02`	`X`	`SPA`	`@0 Péptido @5 02`
C03	`03`	`X`	`FRE`	`@0 Orge @5 03`
C03	`03`	`X`	`ENG`	`@0 Barley @5 03`
C03	`03`	`X`	`SPA`	`@0 Cebada @5 03`
C03	`04`	`X`	`FRE`	`@0 Feuille végétal @5 04`
C03	`04`	`X`	`ENG`	`@0 Plant leaf @5 04`
C03	`04`	`X`	`SPA`	`@0 Hoja vegetal @5 04`
C03	`05`	`X`	`FRE`	`@0 Vacuole @5 05`
C03	`05`	`X`	`ENG`	`@0 Vacuole @5 05`
C03	`05`	`X`	`SPA`	`@0 Vacuola @5 05`
C03	`06`	`X`	`FRE`	`@0 Botanique @5 06`
C03	`06`	`X`	`ENG`	`@0 Botany @5 06`
C03	`06`	`X`	`SPA`	`@0 Botánica @5 06`
C03	`07`	`X`	`FRE`	`@0 Hordeum vulgare @2 NS @5 10`
C03	`07`	`X`	`ENG`	`@0 Hordeum vulgare @2 NS @5 10`
C03	`07`	`X`	`SPA`	`@0 Hordeum vulgare @2 NS @5 10`
C03	`08`	`X`	`FRE`	`@0 Chaîne longue @5 15`
C03	`08`	`X`	`ENG`	`@0 Long chain @5 15`
C03	`08`	`X`	`SPA`	`@0 Cadena larga @5 15`
C03	`09`	`X`	`FRE`	`@0 Transporteur ABC @5 16`
C03	`09`	`X`	`ENG`	`@0 ABC transporter @5 16`
C03	`09`	`X`	`SPA`	`@0 Transportador ABC @5 16`
C03	`10`	`X`	`FRE`	`@0 Mésophylle @4 CD @5 96`
C03	`10`	`X`	`ENG`	`@0 Mesophyll @4 CD @5 96`
C07	`01`	`X`	`FRE`	`@0 Gramineae @2 NS`
C07	`01`	`X`	`ENG`	`@0 Gramineae @2 NS`
C07	`01`	`X`	`SPA`	`@0 Gramineae @2 NS`
C07	`02`	`X`	`FRE`	`@0 Monocotyledones @2 NS`
C07	`02`	`X`	`ENG`	`@0 Monocotyledones @2 NS`
C07	`02`	`X`	`SPA`	`@0 Monocotyledones @2 NS`
C07	`03`	`X`	`FRE`	`@0 Angiospermae @2 NS`
C07	`03`	`X`	`ENG`	`@0 Angiospermae @2 NS`
C07	`03`	`X`	`SPA`	`@0 Angiospermae @2 NS`
C07	`04`	`X`	`FRE`	`@0 Spermatophyta @2 NS`
C07	`04`	`X`	`ENG`	`@0 Spermatophyta @2 NS`
C07	`04`	`X`	`SPA`	`@0 Spermatophyta @2 NS`
C07	`05`	`X`	`FRE`	`@0 Plante céréalière @5 31`
C07	`05`	`X`	`ENG`	`@0 Cereal crop @5 31`
C07	`05`	`X`	`SPA`	`@0 Planta cerealista @5 31`
N21				`@1 171`
N44	`01`			`@1 OTO`
N82				`@1 OTO`

Format Inist (serveur)

NO :	PASCAL 11-0251115 INIST
ET :	Characterization of a transport activity for long-chain peptides in barley mesophyll vacuoles
AU :	SCHNELL RAMOS (Magali); ABELE (Rupert); NAGY (Reka); SUTER GROTEMEYER (Marianne); TAMPE (Robert); RENTSCH (Doris); MARTINOIA (Enrico); GILLIHAM (M.)
AF :	Institute of Plant Biology, University Zurich, Zollikerstrasse 107/8008 Zurich/Suisse (1 aut., 3 aut., 7 aut.); Institute of Biochemistry, Biocenter, Goethe-University Frankfurt, Max-von-Laue Strasse 9 9/60438 Frankfurt am Main/Allemagne (2 aut., 5 aut.); Institute of Plant Sciences, University of Bern, Altenbergrain 21/3013 Bern/Suisse (4 aut., 6 aut.); Institut des Sciences du Végétal, CNRS, 1, av. de la Terrasse/91198 Gif-sur-Yvette/France (1 aut.); School of Agriculture, Food and Wine & Waite Research Institute, University of Adelaide/Australie (1 aut.)
DT :	Publication en série; Papier de recherche; Niveau analytique
SO :	Journal of experimental botany; ISSN 0022-0957; Coden JEBOA6; Royaume-Uni; Da. 2011; Vol. 62; No. 7; Pp. 2403-2410; Bibl. 1 p.
LA :	Anglais
EA :	The plant vacuole is the largest compartment in a fully expanded plant cell. While only very limited metabolic activity can be observed within the vacuole, the majority of the hydrolytic activities, including proteolytic activities reside in this organelle. Since it is assumed that protein degradation by the proteasome results in the production of peptides with a size of 3-30 amino acids, we were interested to show whether the tonoplast exhibits a transport activity, which could deliver these peptides into the vacuole for final degradation. It is shown here that isolated barley mesophyll vacuoles take up peptides of 9-27 amino acids in a strictly ATP-dependent manner. Uptake is inhibited by vanadate, but not by NH⁺₄, while GTP could partially substitute for ATP. The apparent affinity for the 9 amino acid peptide was 15 μM, suggesting that peptides are efficiently transferred to the vacuole in vivo. Inhibition experiments showed that peptides with a chain length below 10 amino acids did not compete as efficiently as longer peptides for the uptake of the 9 amino acid peptide. Our results suggest that vacuoles contain at least one peptide transporter that belongs to the ABC-type transporters, which efficiently exports long-chain peptides from the cytosol into the vacuole for final degradation.
CC :	002A10
FD :	Transport; Peptide; Orge; Feuille végétal; Vacuole; Botanique; Hordeum vulgare; Chaîne longue; Transporteur ABC; Mésophylle
FG :	Gramineae; Monocotyledones; Angiospermae; Spermatophyta; Plante céréalière
ED :	Transport; Peptides; Barley; Plant leaf; Vacuole; Botany; Hordeum vulgare; Long chain; ABC transporter; Mesophyll
EG :	Gramineae; Monocotyledones; Angiospermae; Spermatophyta; Cereal crop
SD :	Transporte; Péptido; Cebada; Hoja vegetal; Vacuola; Botánica; Hordeum vulgare; Cadena larga; Transportador ABC
LO :	INIST-6923.354000191483460140
ID :	11-0251115

Links to Exploration step

Pascal:11-0251115

Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>ABC transporter</term>
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<term>Peptide</term>
<term>Orge</term>
<term>Feuille végétal</term>
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<term>Hordeum vulgare</term>
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<front><div type="abstract" xml:lang="en">The plant vacuole is the largest compartment in a fully expanded plant cell. While only very limited metabolic activity can be observed within the vacuole, the majority of the hydrolytic activities, including proteolytic activities reside in this organelle. Since it is assumed that protein degradation by the proteasome results in the production of peptides with a size of 3-30 amino acids, we were interested to show whether the tonoplast exhibits a transport activity, which could deliver these peptides into the vacuole for final degradation. It is shown here that isolated barley mesophyll vacuoles take up peptides of 9-27 amino acids in a strictly ATP-dependent manner. Uptake is inhibited by vanadate, but not by NH<sup>+</sup>
<sub>4</sub>
, while GTP could partially substitute for ATP. The apparent affinity for the 9 amino acid peptide was 15 μM, suggesting that peptides are efficiently transferred to the vacuole in vivo. Inhibition experiments showed that peptides with a chain length below 10 amino acids did not compete as efficiently as longer peptides for the uptake of the 9 amino acid peptide. Our results suggest that vacuoles contain at least one peptide transporter that belongs to the ABC-type transporters, which efficiently exports long-chain peptides from the cytosol into the vacuole for final degradation.</div>
</front>
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<fA11 i1="01" i2="1"><s1>SCHNELL RAMOS (Magali)</s1>
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<fA11 i1="07" i2="1"><s1>MARTINOIA (Enrico)</s1>
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<fA12 i1="01" i2="1"><s1>GILLIHAM (M.)</s1>
<s9>limin.</s9>
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<fA14 i1="01"><s1>Institute of Plant Biology, University Zurich, Zollikerstrasse 107</s1>
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<fA14 i1="02"><s1>Institute of Biochemistry, Biocenter, Goethe-University Frankfurt, Max-von-Laue Strasse 9 9</s1>
<s2>60438 Frankfurt am Main</s2>
<s3>DEU</s3>
<sZ>2 aut.</sZ>
<sZ>5 aut.</sZ>
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<fA14 i1="03"><s1>Institute of Plant Sciences, University of Bern, Altenbergrain 21</s1>
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<s3>CHE</s3>
<sZ>4 aut.</sZ>
<sZ>6 aut.</sZ>
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<fA14 i1="04"><s1>Institut des Sciences du Végétal, CNRS, 1, av. de la Terrasse</s1>
<s2>91198 Gif-sur-Yvette</s2>
<s3>FRA</s3>
<sZ>1 aut.</sZ>
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<s3>AUS</s3>
<sZ>1 aut.</sZ>
</fA15>
<fA20><s1>2403-2410</s1>
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<fC01 i1="01" l="ENG"><s0>The plant vacuole is the largest compartment in a fully expanded plant cell. While only very limited metabolic activity can be observed within the vacuole, the majority of the hydrolytic activities, including proteolytic activities reside in this organelle. Since it is assumed that protein degradation by the proteasome results in the production of peptides with a size of 3-30 amino acids, we were interested to show whether the tonoplast exhibits a transport activity, which could deliver these peptides into the vacuole for final degradation. It is shown here that isolated barley mesophyll vacuoles take up peptides of 9-27 amino acids in a strictly ATP-dependent manner. Uptake is inhibited by vanadate, but not by NH<sup>+</sup>
<sub>4</sub>
, while GTP could partially substitute for ATP. The apparent affinity for the 9 amino acid peptide was 15 μM, suggesting that peptides are efficiently transferred to the vacuole in vivo. Inhibition experiments showed that peptides with a chain length below 10 amino acids did not compete as efficiently as longer peptides for the uptake of the 9 amino acid peptide. Our results suggest that vacuoles contain at least one peptide transporter that belongs to the ABC-type transporters, which efficiently exports long-chain peptides from the cytosol into the vacuole for final degradation.</s0>
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<s2>NS</s2>
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<fC07 i1="04" i2="X" l="FRE"><s0>Spermatophyta</s0>
<s2>NS</s2>
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<s2>NS</s2>
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<fC07 i1="05" i2="X" l="FRE"><s0>Plante céréalière</s0>
<s5>31</s5>
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<fC07 i1="05" i2="X" l="ENG"><s0>Cereal crop</s0>
<s5>31</s5>
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<fC07 i1="05" i2="X" l="SPA"><s0>Planta cerealista</s0>
<s5>31</s5>
</fC07>
<fN21><s1>171</s1>
</fN21>
<fN44 i1="01"><s1>OTO</s1>
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<server><NO>PASCAL 11-0251115 INIST</NO>
<ET>Characterization of a transport activity for long-chain peptides in barley mesophyll vacuoles</ET>
<AU>SCHNELL RAMOS (Magali); ABELE (Rupert); NAGY (Reka); SUTER GROTEMEYER (Marianne); TAMPE (Robert); RENTSCH (Doris); MARTINOIA (Enrico); GILLIHAM (M.)</AU>
<AF>Institute of Plant Biology, University Zurich, Zollikerstrasse 107/8008 Zurich/Suisse (1 aut., 3 aut., 7 aut.); Institute of Biochemistry, Biocenter, Goethe-University Frankfurt, Max-von-Laue Strasse 9 9/60438 Frankfurt am Main/Allemagne (2 aut., 5 aut.); Institute of Plant Sciences, University of Bern, Altenbergrain 21/3013 Bern/Suisse (4 aut., 6 aut.); Institut des Sciences du Végétal, CNRS, 1, av. de la Terrasse/91198 Gif-sur-Yvette/France (1 aut.); School of Agriculture, Food and Wine & Waite Research Institute, University of Adelaide/Australie (1 aut.)</AF>
<DT>Publication en série; Papier de recherche; Niveau analytique</DT>
<SO>Journal of experimental botany; ISSN 0022-0957; Coden JEBOA6; Royaume-Uni; Da. 2011; Vol. 62; No. 7; Pp. 2403-2410; Bibl. 1 p.</SO>
<LA>Anglais</LA>
<EA>The plant vacuole is the largest compartment in a fully expanded plant cell. While only very limited metabolic activity can be observed within the vacuole, the majority of the hydrolytic activities, including proteolytic activities reside in this organelle. Since it is assumed that protein degradation by the proteasome results in the production of peptides with a size of 3-30 amino acids, we were interested to show whether the tonoplast exhibits a transport activity, which could deliver these peptides into the vacuole for final degradation. It is shown here that isolated barley mesophyll vacuoles take up peptides of 9-27 amino acids in a strictly ATP-dependent manner. Uptake is inhibited by vanadate, but not by NH<sup>+</sup>
<sub>4</sub>
, while GTP could partially substitute for ATP. The apparent affinity for the 9 amino acid peptide was 15 μM, suggesting that peptides are efficiently transferred to the vacuole in vivo. Inhibition experiments showed that peptides with a chain length below 10 amino acids did not compete as efficiently as longer peptides for the uptake of the 9 amino acid peptide. Our results suggest that vacuoles contain at least one peptide transporter that belongs to the ABC-type transporters, which efficiently exports long-chain peptides from the cytosol into the vacuole for final degradation.</EA>
<CC>002A10</CC>
<FD>Transport; Peptide; Orge; Feuille végétal; Vacuole; Botanique; Hordeum vulgare; Chaîne longue; Transporteur ABC; Mésophylle</FD>
<FG>Gramineae; Monocotyledones; Angiospermae; Spermatophyta; Plante céréalière</FG>
<ED>Transport; Peptides; Barley; Plant leaf; Vacuole; Botany; Hordeum vulgare; Long chain; ABC transporter; Mesophyll</ED>
<EG>Gramineae; Monocotyledones; Angiospermae; Spermatophyta; Cereal crop</EG>
<SD>Transporte; Péptido; Cebada; Hoja vegetal; Vacuola; Botánica; Hordeum vulgare; Cadena larga; Transportador ABC</SD>
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Characterization of a transport activity for long-chain peptides in barley mesophyll vacuoles

Characterization of a transport activity for long-chain peptides in barley mesophyll vacuoles

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