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Plant Cell, Vol. 12, 419-432, March 2000, Copyright © 2000, American Society of Plant Physiologists

The Thylakoid FtsH Protease Plays a Role in the Light-Induced Turnover of the Photosystem II D1 Protein

Marika Lindahla, Cornelia Speteab,c, Torill Hundalb,c, Amos B. Oppenheimd, Zach Adama, and Bertil Anderssonb,c
a Department of Agricultural Botany, Hebrew University of Jerusalem, Rehovot 76100, Israel
b Department of Biochemistry, Arrhenius Laboratories for Natural Sciences, Stockholm University, S-10691 Stockholm, Sweden
c Division of Cell Biology, Linköping University, SE-58185 Linköping, Sweden
d Department of Molecular Genetics and Biotechnology, Hebrew University of Jerusalem, Jerusalem 91010, Israel

Correspondence to: Zach Adam, zach{at}agri.huji.ac.il (E-mail), 972-8-946-7763 (fax)

The photosystem II reaction center D1 protein is known to turn over frequently. This protein is prone to irreversible damage caused by reactive oxygen species that are formed in the light; the damaged, nonfunctional D1 protein is degraded and replaced by a new copy. However, the proteases responsible for D1 protein degradation remain unknown. In this study, we investigate the possible role of the FtsH protease, an ATP-dependent zinc metalloprotease, during this process. The primary light-induced cleavage product of the D1 protein, a 23-kD fragment, was found to be degraded in isolated thylakoids in the dark during a process dependent on ATP hydrolysis and divalent metal ions, suggesting the involvement of FtsH. Purified FtsH degraded the 23-kD D1 fragment present in isolated photosystem II core complexes, as well as that in thylakoid membranes depleted of endogenous FtsH. In this study, we definitively identify the chloroplast protease acting on the D1 protein during its light-induced turnover. Unlike previously identified membrane-bound substrates for FtsH in bacteria and mitochondria, the 23-kD D1 fragment represents a novel class of FtsH substrate—functionally assembled proteins that have undergone irreversible photooxidative damage and cleavage.




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