Identification and biochemical characterization of the plasma-membrane H+-ATPase in guard cells of Vicia faba L.

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Autoren

  • Dirk Becker
  • Carsten Zeilinger
  • Gabi Lohse
  • Hans Depta
  • Rainer Hedrich

Externe Organisationen

  • Georg-August-Universität Göttingen
Forschungs-netzwerk anzeigen

Details

OriginalspracheEnglisch
Seiten (von - bis)44-50
Seitenumfang7
FachzeitschriftPLANTA
Jahrgang190
Ausgabenummer1
PublikationsstatusVeröffentlicht - Mai 1993

Abstract

The plasma-membrane H+-pump in guard cells generates the driving force for the rapid ion fluxes required for stomatal opening. Since our electrophysio-logical studies revealed a two fold higher pump-current density in guard cells than in mesophyll cells of Vicia faba L. we elucidated the biochemical properties of this proton-translocating ATPase in plasma-membrane vesicles isolated from both cell types. The capability of the H+ -ATPase to create an H+ gradient is maintained in plasma-membrane vesicles derived from purified guard cells via blender maceration, high-pressure homogenization and polymer separation. The H+-pumping activity of these vesicles coincides with the presence of two polypeptides of approx. 100 and 92 kDa which are recognized by a monoclonal antibody raised against the plasma-membrane H+-ATPase from Zea mays L. coleoptiles. Comparison of H+-pumping activities of isolated membranes revealed an approximately two fold higher activity in guard cells than in mesophyll cells with respect to the total membrane protein content. Furthermore, we demonstrated by western blotting that the difference in pump activities resulted from a higher abundance of the electroenzyme per unit membrane protein in guard-cell plasma membranes. We suggest that the high H+-pump capacity is necessary to enable guard cells to respond to sudden changes in the environment by a change in stomatal aperture.

ASJC Scopus Sachgebiete

  • Biochemie, Genetik und Molekularbiologie (insg.)
  • Genetik
  • Agrar- und Biowissenschaften (insg.)
  • Pflanzenkunde

Zitieren

Identification and biochemical characterization of the plasma-membrane H+-ATPase in guard cells of Vicia faba L. / Becker, Dirk; Zeilinger, Carsten; Lohse, Gabi et al.
in: PLANTA, Jahrgang 190, Nr. 1, 05.1993, S. 44-50.

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Becker D, Zeilinger C, Lohse G, Depta H, Hedrich R. Identification and biochemical characterization of the plasma-membrane H+-ATPase in guard cells of Vicia faba L. PLANTA. 1993 Mai;190(1):44-50. doi: 10.1007/BF00195673
Becker, Dirk ; Zeilinger, Carsten ; Lohse, Gabi et al. / Identification and biochemical characterization of the plasma-membrane H+-ATPase in guard cells of Vicia faba L. in: PLANTA. 1993 ; Jahrgang 190, Nr. 1. S. 44-50.
Download
@article{d962577fc7a74048b54684583e1f9be7,
title = "Identification and biochemical characterization of the plasma-membrane H+-ATPase in guard cells of Vicia faba L.",
abstract = "The plasma-membrane H+-pump in guard cells generates the driving force for the rapid ion fluxes required for stomatal opening. Since our electrophysio-logical studies revealed a two fold higher pump-current density in guard cells than in mesophyll cells of Vicia faba L. we elucidated the biochemical properties of this proton-translocating ATPase in plasma-membrane vesicles isolated from both cell types. The capability of the H+ -ATPase to create an H+ gradient is maintained in plasma-membrane vesicles derived from purified guard cells via blender maceration, high-pressure homogenization and polymer separation. The H+-pumping activity of these vesicles coincides with the presence of two polypeptides of approx. 100 and 92 kDa which are recognized by a monoclonal antibody raised against the plasma-membrane H+-ATPase from Zea mays L. coleoptiles. Comparison of H+-pumping activities of isolated membranes revealed an approximately two fold higher activity in guard cells than in mesophyll cells with respect to the total membrane protein content. Furthermore, we demonstrated by western blotting that the difference in pump activities resulted from a higher abundance of the electroenzyme per unit membrane protein in guard-cell plasma membranes. We suggest that the high H+-pump capacity is necessary to enable guard cells to respond to sudden changes in the environment by a change in stomatal aperture.",
keywords = "Guard cell, H-ATPase, Mesophyll cell, Patch-clamp, Plasma membrane, Proton pump (membrane density)",
author = "Dirk Becker and Carsten Zeilinger and Gabi Lohse and Hans Depta and Rainer Hedrich",
year = "1993",
month = may,
doi = "10.1007/BF00195673",
language = "English",
volume = "190",
pages = "44--50",
journal = "PLANTA",
issn = "0032-0935",
publisher = "Springer Verlag",
number = "1",

}

Download

TY - JOUR

T1 - Identification and biochemical characterization of the plasma-membrane H+-ATPase in guard cells of Vicia faba L.

AU - Becker, Dirk

AU - Zeilinger, Carsten

AU - Lohse, Gabi

AU - Depta, Hans

AU - Hedrich, Rainer

PY - 1993/5

Y1 - 1993/5

N2 - The plasma-membrane H+-pump in guard cells generates the driving force for the rapid ion fluxes required for stomatal opening. Since our electrophysio-logical studies revealed a two fold higher pump-current density in guard cells than in mesophyll cells of Vicia faba L. we elucidated the biochemical properties of this proton-translocating ATPase in plasma-membrane vesicles isolated from both cell types. The capability of the H+ -ATPase to create an H+ gradient is maintained in plasma-membrane vesicles derived from purified guard cells via blender maceration, high-pressure homogenization and polymer separation. The H+-pumping activity of these vesicles coincides with the presence of two polypeptides of approx. 100 and 92 kDa which are recognized by a monoclonal antibody raised against the plasma-membrane H+-ATPase from Zea mays L. coleoptiles. Comparison of H+-pumping activities of isolated membranes revealed an approximately two fold higher activity in guard cells than in mesophyll cells with respect to the total membrane protein content. Furthermore, we demonstrated by western blotting that the difference in pump activities resulted from a higher abundance of the electroenzyme per unit membrane protein in guard-cell plasma membranes. We suggest that the high H+-pump capacity is necessary to enable guard cells to respond to sudden changes in the environment by a change in stomatal aperture.

AB - The plasma-membrane H+-pump in guard cells generates the driving force for the rapid ion fluxes required for stomatal opening. Since our electrophysio-logical studies revealed a two fold higher pump-current density in guard cells than in mesophyll cells of Vicia faba L. we elucidated the biochemical properties of this proton-translocating ATPase in plasma-membrane vesicles isolated from both cell types. The capability of the H+ -ATPase to create an H+ gradient is maintained in plasma-membrane vesicles derived from purified guard cells via blender maceration, high-pressure homogenization and polymer separation. The H+-pumping activity of these vesicles coincides with the presence of two polypeptides of approx. 100 and 92 kDa which are recognized by a monoclonal antibody raised against the plasma-membrane H+-ATPase from Zea mays L. coleoptiles. Comparison of H+-pumping activities of isolated membranes revealed an approximately two fold higher activity in guard cells than in mesophyll cells with respect to the total membrane protein content. Furthermore, we demonstrated by western blotting that the difference in pump activities resulted from a higher abundance of the electroenzyme per unit membrane protein in guard-cell plasma membranes. We suggest that the high H+-pump capacity is necessary to enable guard cells to respond to sudden changes in the environment by a change in stomatal aperture.

KW - Guard cell

KW - H-ATPase

KW - Mesophyll cell

KW - Patch-clamp

KW - Plasma membrane

KW - Proton pump (membrane density)

UR - http://www.scopus.com/inward/record.url?scp=0002617899&partnerID=8YFLogxK

U2 - 10.1007/BF00195673

DO - 10.1007/BF00195673

M3 - Article

AN - SCOPUS:0002617899

VL - 190

SP - 44

EP - 50

JO - PLANTA

JF - PLANTA

SN - 0032-0935

IS - 1

ER -