Proteomic and functional characterization of a Chlamydomonas reinhardtii mutant lacking the mitochondrial alternative oxidase 1.

Abstract

In the present work, we have isolated by RNA interference and characterized at the functional and the proteomic levels a Chlamydomonas reinhardtii strain devoid of the mitochondrial alternative oxidase 1 (AOX1). The AOX1-deficient strain displays a remarkable doubling of the cell volume and biomass without alteration of the generation time or change in total respiratory rate, with a significantly higher ROS production. To identify the molecular adaptation underlying these observations, we have carried out a comparative study of both the mitochondrial and the cellular soluble proteomes. Our results indicate a strong up-regulation of the ROS scavenging systems and important quantitative modifications of proteins involved in the primary metabolism, namely an increase of enzymes involved in anabolic pathways and a concomitant general down-regulation of enzymes of the main catabolic pathways.

DOI: 10.1021/pr900866e

Cite this paper

@article{Mathy2010ProteomicAF, title={Proteomic and functional characterization of a Chlamydomonas reinhardtii mutant lacking the mitochondrial alternative oxidase 1.}, author={Gr{\'e}gory Mathy and Pierre Cardol and Monique Dinant and Arnaud Blomme and St{\'e}phanie G{\'e}rin and Marie Cloes and Bart Ghysels and Edwin Depauw and Pierre Leprince and Claire Remacle and Claudine M. Sluse-Goffart and Fabrice Franck and Ren{\'e} Fernand Matagne and Francis E. Sluse}, journal={Journal of proteome research}, year={2010}, volume={9 6}, pages={2825-38} }