Plant Physiology Preview
Published on April 3, 2003; 10.1104/pp.102.018325
Received November 25, 2002
Returned for revision December 18, 2002
Accepted January 30, 2003
Identification of Novel Mitochondrial Protein Components of Chlamydomonas reinhardtii. A Proteomic Approach
Robert van Lis , Ariane Atteia , Guillermo Mendoza-Hernández , and Diego González-Halphen *
Departamento de Genética Molecular, Instituto de Fisiología Celular (R.v.L., A.A., D.G.-H.) and Departamento de Bioquímica, Facultad de Medicina (G.M.-H.), Universidad Nacional Autónoma de México, 04510 Mexico D.F., Mexico
* Corresponding author; email: dhalphen{at}ifisiol.unam.mx.
Pure mitochondria of the photosynthetic alga Chlamydomonas reinhardtii were analyzed using blue native-polyacrylamide gel electrophoresis (BN-PAGE). The major oxidative phosphorylation complexes were resolved: F1F0-ATP synthase, NADH-ubiquinone oxidoreductase, ubiquinol-cytochrome c reductase, and cytochrome c oxidase. The oligomeric states of these complexes were determined. The F1F0-ATP synthase runs exclusively as a dimer, in contrast to the C. reinhardtii chloroplast enzyme, which is present as a monomer and subcomplexes. The sequence of a 60-kD protein, associated with the mitochondrial ATP synthase and with no known counterpart in any other organism, is reported. This protein may be related to the strong dimeric character of the algal F1F0-ATP synthase. The oxidative phosphorylation complexes resolved by BN-PAGE were separated into their subunits by second dimension sodium dodecyl sulfate-PAGE. A number of polypeptides were identified mainly on the basis of their N-terminal sequence. Core I and II subunits of complex III were characterized, and their proteolytic activities were predicted. Also, the heterodimeric nature of COXIIA and COXIIB subunits in cytochrome c oxidase was demonstrated. Other mitochondrial proteins like the chaperone HSP60, the alternative oxidase, the aconitase, and the ADP/ATP carrier were identified. BN-PAGE was also used to approach the analysis of the major chloroplast protein complexes of C. reinhardtii.
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