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J Biol Chem, Vol. 275, Issue 10, 7205-7211, March 10, 2000
From the 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.
GTP Enhances the Degradation of the Photosystem II D1 Protein
Irrespective of Its Conformational Heterogeneity at the QB
Site*
§,
§,
,
§
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
*
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.
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