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J Biol Chem, Vol. 275, Issue 10, 7205-7211, March 10, 2000

GTP Enhances the Degradation of the Photosystem II D1 Protein Irrespective of Its Conformational Heterogeneity at the QB Site*

Cornelia SpeteaDagger §, Nir Keren, Torill HundalDagger §, Jean-Michel DoanDagger ||, Itzhak Ohad**, and Bertil AnderssonDagger §

From the Dagger  Department of Biochemistry, Arrhenius Laboratories for Natural Sciences, Stockholm University, Stockholm SE-106 91, Sweden, the § Division of Cell Biology, Linköping University, Linköping SE-581 85, Sweden, the  Department of Biological Chemistry, The Hebrew University of Jerusalem, Jerusalem 91904, Israel, and || Department of Cell Biology, University Pierre and Marie Curie, Paris 75005, France

The light exposure history and/or binding of different herbicides at the QB site may induce heterogeneity of photosystem II acceptor side conformation that affects D1 protein degradation under photoinhibitory conditions. GTP was recently found to stimulate the D1 protein degradation of photoinactivated photosystem II (Spetea, C., Hundal, T., Lohmann, F., and Andersson, B. (1999) Proc. Natl. Acad. Sci. U. S. A. 96, 6547-6552). Here we report that GTP enhances the cleavage of the D1 protein D-E loop following exposure of thylakoid membranes to either high light, low light, or repetitive single turnover flashes but not to trypsin. GTP does not stimulate D1 protein degradation in the presence of herbicides known to affect the accessibility of the cleavage site to proteolysis. However, GTP stimulates degradation that can be induced even in darkness in some photosystem II conformers following binding of the PNO8 herbicide (Nakajima, Y., Yoshida, S., Inoue, Y., Yoneyama, K., and Ono, T. (1995) Biochim. Biophys. Acta 1230, 38-44). Both the PNO8- and the light-induced primary cleavage of the D1 protein occur in the grana membrane domains. The subsequent migration of photosytem II containing the D1 protein fragments to the stroma domains for secondary proteolysis is light-activated. We conclude that the GTP effect is not confined to a specific photoinactivation pathway nor to the conformational state of the photosytem II acceptor side. Consequently, GTP does not interact with the site of D1 protein cleavage but rather enhances the activity of the endogenous proteolytic system.


* This work was supported by grants from the Swedish Natural Science Research Council and Human Frontiers Science Program. The experiments using single turnover flashes were performed in the Jerusalem laboratory and were supported by the German-Israeli Foundation and the Minerva-Avron Center for Photosynthesis Research.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

** Has spent a sabbatical period in the Stockholm laboratory, supported by the Nobel Committee for Chemistry. To whom correspondence should be addressed. Tel.: +972-2-6585423; Fax: +972-2-6586448; E-mail: ohad@vms.huji.ac.il.


Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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