A metalloprotease involved in the processing of mitochondrial precursor proteins

Abstract

A protease that cleaves the precursor of ornithine carbamoyltransferase (EC 2.1.3.3), a mitochondrial matrix enzyme, has been partially purified from the matrix fraction of rat liver mitochondria. The protease cleaved the precursors of several other matrix proteins at apparently correct sites. The protease was inhibited by 1,10-phenanthroline and EDTA, was reactivated by excess Mn2+ or Co2+, and did not cleave the alkali-denatured precursor proteins. These and other results indicate that this protease is responsible for the processing of at least several matrix protein precursors, and that the enzyme recognizes some three-dimensional conformation of the precursors as well as the amino acid sequences around the cleavage sites. © 1986.