Biosynthesis of the ubiquinol‐cytochrome c reductase complex in yeast

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Abstract
The mitochondrial ubiquinol--cytochrome c reductase complex (complex III or cytochrome bc1 complex) is thought to consist of eight subunits, seven of which are specified by nuclear genes and synthesized in the cytoplasm. We have studied the synthesis of five of the nuclear-encoded subunits both in vivo and in vitro and show that of these the 44-kDa, 40-kDa and 17-kDa subunits are synthesized with cleavable extensions, while the 14-kDa and 11-kDa proteins are synthesized without detectable extra sequences. The sizes of the pre-sequences, as determined by the relative mobility of the precursor proteins in sodium dodecyl sulphate/polyacrylamide gels, range from 0.5-kDa for the 44-kDa and 40-kDa subunits to 9-kDa for the 17-kDa subunit. The existence in vivo of precursor forms to the 44-kDa, 40-kDa and 17-kDa subunits implies that import is at least partially a post-translational process. The precursor of the 44-kDa subunit can be processed post-translationally in vitro by isolated mitochondria. The messenger RNAs for subunits of the complex have been studied. Those coding for the 44-kDa, 40-kDa, 14-kDa and 11-kDa proteins and cytochrome c1 are of different sizes, indicating that each of these subunits is synthesized as a separate protein, rather than as part of a polyprotein precursor.