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J. Biol. Chem., Vol. 266, Issue 15, 9932-9938, May, 1991

Effect of oxygen on the synthesis and assembly of mitochondrial encoded subunits of cytochrome oxidase and cytochrome b.c1 in mouse embryo fibroblasts

MA Asson-Batres and JF Hare
Department of Biochemistry and Molecular Biology, Oregon Health Sciences University, Portland 97201.

Mouse embryo fibroblasts were grown in low and control O2 for 24 h (average medium oxygen tensions, 7 torr and 143 torr, respectively). Relative to controls, there was a reduction in radiolabeled subunits in immunoprecipitates of cytochrome oxidase and cytochrome b.c1 prepared from low O2 cells. Incorporation of radiolabeled amino acids into subunit I of cytochrome oxidase and the apocytochrome b protein of the b.c1 complex ranged from 51-100% of control, whereas the appearance of these pulse-labeled subunits into holoenzymes immunoprecipitated from low O2 cells was in the range of 6-39% of control. The synthesis of subunit II of cytochrome oxidase by low O2 cells ranged from 63-100% of control, and assembly of this protein into the low O2 immunoprecipitated enzyme ranged from 15-61% of control. Thus, the data suggest that O2 had an effect on the assembly of these mitochondrially translated proteins that was independent of any effect on their synthesis.
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