The role of 3' UTRs in the mechanisms for segregating mitochondrial proteins

The mitochondrial proteome, meant as the collection of proteins localized in the mitochondrion, whose fundamental function is the energy production for the life of the cell, is estimated to be constituted by at least 1000 proteins. Since the mitochondrial genome codes only for 13 polypeptides, in practice all of them are coded by nuclear genes and are imported in the mitochondrion by means of a sophisticated mechanism of sorting that is not completely known. Most classified mitochondrial proteins are synthesized as precursors with an amino-terminal extension (leader peptide), provided with peculiar physical and structural characteristics that are responsible for the recognition and import system. However, there is experimental evidence that complementary or alternative import systems exist. In particular, the 3' UnTranslated Regions (UTRs) of the mRNAs may be involved, through their secondary structure, in the mechanisms of recognition and localization. In this paper, the information content of different human mRNA sequences has been analyzed, and the results show that a significative short-term correlation exists in the 3' UTR sequences of the mRNA's coding for the proteins provided with leader peptides, probably representing the structural constraints that are necessary to the sorting machinery.