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THE PLANT CELL, Vol 5, Issue 12 1865-1876, Copyright © 1993 by American Society of Plant Biologists
Newly Imported Rieske Iron-Sulfur Protein Associates with Both Cpn60 and Hsp70 in the Chloroplast Stroma
F. Madueno, J. A. Napier and J. C. Gray
Department of Plant Sciences and Cambridge Centre for Molecular Recognition, University of Cambridge, Downing Street, Cambridge CB2 3EA, United Kingdom
The precursor of the Rieske FeS protein, a thylakoid membrane protein, was
imported by isolated pea chloroplasts, and the mature protein was shown to
be integrated into the cytochrome bf complex of the thylakoid membranes.
Insertion into the thylakoid membrane was sensitive to the ionophores
nigericin and valinomycin, suggesting a requirement for a proton motive
force. A considerable proportion of the imported Rieske protein was
detected in the stromal fraction of the chloroplasts, and this increased
when membrane insertion was blocked with ionophores. Electrophoresis of the
stromal fraction under nondenaturing conditions resolved two distinct
complexes containing the Rieske protein. One of these complexes was
identified as an association of the Rieske protein with the chaperonin
Cpn60 complex by its electrophoretic mobility, Mg-ATP-dependent
dissociation, and immunoprecipitation with anti-Cpn60 antibodies.
Coimmunoprecipitation of imported Rieske protein with anti-heat shock
protein 70 (Hsp70) antibodies indicated that the Rieske protein was also
associated, in an ATP-dissociable form, with a chloroplast Hsp70 homolog.
Immunoprecipitation analysis of an import time course detected the highest
amounts of the Cpn60-Rieske protein complex early in the time course,
whereas highest amounts of the Hsp70-Rieske protein complex were formed
much later. The disappearance of the Cpn60-Rieske protein complex
correlated with increased amounts of the Rieske protein in the thylakoid
fraction.
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