Som1, a third component of the yeast mitochondrial inner membrane peptidase complex that contains Imp1 and Imp2

The mitochondrial inner membrane peptidase Imp is required for proteolytic processing of the mitochondrially encoded protein Cox2, the nucleus-encoded Cyt b(2), Mcr1, and Cyt c(1), and possibly other proteins, during their tr ansport across the mitochondrial membranes. The peptidase contains two cata lytic subunits, Imp1 and Imp2. The small protein Som1 was previously shown to affect the function of Imp1? but the precise role of Som1 remained unkno wn. Using mutants deleted for IMP1, IMP2 and SOM1, we show here that the So m1 protein is absent in the imp1 Delta mutant, whereas the level of the Imp 1 subunit of the peptidase is only slightly reduced in the som1 null mutant . The Som1 protein is not essential for proteolytic processing of Cyt b(2), while the two other known Imp1 substrates. Cox2 and Mcr1, are not processe d in the absence of Semi. Proteolytic processing of Cyt c(1) by the Imp2 su bunit, and of Ccp by an as yet unidentified peptidase, is not impaired in t he som1 deletion mutant. By crosslinking and co-immunoprecipitation assays we demonstrate that the Imp1 and Som1 proteins physically interact. We conc lude from our results that stabilisation of Som1 and correct Imp1 function is mediated by a direct interaction between the Imp1 and Som1 proteins, sug gesting that Som1 represents a third subunit of the Imp peptidase complex.