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Plant Cell, Vol. 12, 137-150, January 2000, Copyright © 2000, American Society of Plant Physiologists

Evidence for a Role of ClpP in the Degradation of the Chloroplast Cytochrome b6f Complex

Wojciech Majerana, Françis-André Wollmana, and Olivier Vallona
a Centre National de la Recherche Scientifique (CNRS) UPR 1261, Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, F-75005 Paris, France

Correspondence to: Olivier Vallon, vallon{at}ibpc.fr (E-mail), 33-1-46-33-43-03 (fax)

In the green alga Chlamydomonas reinhardtii, the ClpP protease is encoded by an essential chloroplast gene. Mutating its AUG translation initiation codon to AUU reduced ClpP accumulation to 25 to 45% of that of the wild type. Both the mature protein and the putative precursor containing its insertion sequence were present in reduced amounts. Attenuation of ClpP did not affect growth rates under normal conditions but restricted the ability of the cells to adapt to elevated CO2 levels. It also affected the rate of degradation of the cytochrome b6f complex of the thylakoid membrane in two experimental situations: (1) during nitrogen starvation, and (2) in mutants deficient in the Rieske iron–sulfur protein. The ClpP level also controls the steady state accumulation of a mutated version of the Rieske protein. In contrast, attenuation of ClpP did not rescue the fully unassembled subunits in other cytochrome b6f mutants. We conclude that proteolytic disposal of fully or partially assembled cytochrome b6f is controlled by the Clp protease.




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