Plant Physiol.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Web of Science (67)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lanfermeijer, F. C.
Right arrow Articles by Prins, HBA.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lanfermeijer, F. C.
Right arrow Articles by Prins, HBA.
Agricola
Right arrow Articles by Lanfermeijer, F. C.
Right arrow Articles by Prins, HBA.

PLANT PHYSIOLOGY , Vol 104, Issue 4 1277-1285, Copyright © 1994 by American Society of Plant Biologists

METABOLISM AND ENZYMOLOGY

Modulation of H+-ATPase Activity by Fusicoccin in Plasma Membrane Vesicles from Oat (Avena sativa L.) Roots (A Comparison of Modulation by Fusicoccin, Trypsin, and Lysophosphatidylcholine)

F. C. Lanfermeijer and HBA. Prins
Department of Plant Biology, University of Groningen, P.O. Box 14, NL-9750 AA, Haren, The Netherlands

The fungal phytotoxin fusicoccin affects various transport processes in the plasma membrane of plant cells. The plasma membrane (PM) H+-ATPase (EC 3.6.1.35) seems to be the primary target of fusicoccin action. The kinetics of the stimulation of the PM H+-ATPase by fusicoccin was studied in PM vesicles isolated from oat (Avena sativa cv Adamo) roots by aqueous two-phase partitioning. Considerable stimulation of activity was observed only when roots were treated with fusicoccin prior to the PM isolation. Fusicoccin treatment shifted the pH optimum of the ATPase toward more alkaline values and increased Vmax. No effects on Km were observed. Treatment with trypsin resulted in stimulation of ATPase activity in control vesicles but not in the fusicoccin-treated vesicles. The characteristics of stimulation by trypsin in control vesicles were comparable with those of stimulation by fusicoccin. This result and the change of the polypeptide pattern on western blots suggest the involvement of the C-terminal inhibitory domain in the fusicoccin signal transduction chain. On the other hand, stimulation by lyso-PC demonstrated other characteristics than stimulation by fusicoccin. Lyso-PC was able to stimulate ATPase activity at both acidic and alkaline pH values. Kinetic analysis of the pH dependency curves revealed different mechanisms for activation by fusicoccin and by lyso-PC. Whereas fusicoccin shifted the pH dependency of formation of phosphorylated intermediate to more alkaline values, lyso-PC seemed to increase dephosphorylation independently of pH.


This article has been cited by other articles:


Home page
 Plant Cell PhysiolHome page
M. Alsterfjord, P. C. Sehnke, A. Arkell, H. Larsson, F. Svennelid, M. Rosenquist, R. J. Ferl, M. Sommarin, and C. Larsson
Plasma Membrane H+-ATPase and 14-3-3 Isoforms of Arabidopsis Leaves: Evidence for Isoform Specificity in the 14-3-3/H+-ATPase Interaction
Plant Cell Physiol., September 15, 2004; 45(9): 1202 - 1210.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. Jelich-Ottmann, E. W. Weiler, and C. Oecking
Binding of Regulatory 14-3-3 Proteins to the C Terminus of the Plant Plasma Membrane H+-ATPase Involves Part of Its Autoinhibitory Region
J. Biol. Chem., October 19, 2001; 276(43): 39852 - 39857.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. Camoni, V. Iori, M. Marra, and P. Aducci
Phosphorylation-dependent Interaction between Plant Plasma Membrane H+-ATPase and 14-3-3 Proteins
J. Biol. Chem., March 31, 2000; 275(14): 9919 - 9923.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
C. Olivari, C. Albumi, M. C. Pugliarello, and M. I. De Michelis
Phenylarsine Oxide Inhibits the Fusicoccin-Induced Activation of Plasma Membrane H+-ATPase
Plant Physiology, February 1, 2000; 122(2): 463 - 470.
[Abstract] [Full Text]

Home page
 J. Biol. Chem.Home page
M. Piotrowski, P. Morsomme, M. Boutry, and C. Oecking
Complementation of the Saccharomyces cerevisiae Plasma Membrane H+-ATPase by a Plant H+-ATPase Generates a Highly Abundant Fusicoccin Binding Site
J. Biol. Chem., November 6, 1998; 273(45): 30018 - 30023.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
A. Olsson, F. Svennelid, B. Ek, M. Sommarin, and C. Larsson
A Phosphothreonine Residue at the C-Terminal End of the Plasma Membrane H+-ATPase Is Protected by Fusicoccin-Induced 14-3-3 Binding
Plant Physiology, October 1, 1998; 118(2): 551 - 555.
[Abstract] [Full Text]

Home page
 Plant Physiol.Home page
C. Olivari, C. Meanti, M. I. De Michelis, and F. Rasi-Caldogno
Fusicoccin Binding to Its Plasma Membrane Receptor and the Activation of the Plasma Membrane H+-ATPase . IV. Fusicoccin Induces the Association between the Plasma Membrane H+-ATPase and the Fusicoccin Receptor
Plant Physiology, February 1, 1998; 116(2): 529 - 537.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1994 by the American Society of Plant Biologists