J. Biol. Chem., Vol. 263, Issue 12, 5752-5756, Apr, 1988
Structural identity between the NH2-terminal domain of the rat and human ornithine carbamyltransferase "targeting" sequences
C Cote, J Poirier, D Boulet, G Dionne and M Lacroix
Universite du Quebec a Montreal, Department of Chemistry, Canada.
Analysis of the secondary structure of human and rat ornithine
carbamyltransferase's targeting sequence revealed the presence of a highly
homologous domain with the following key features: an hydrophobic patch
opposite to an hydrophilic surface characterized by the disposition of
basic residues at potentially strategic positions. The functional role of
this domain was established using a synthetic peptide corresponding to
amino acids 1-19 of the rat ornithine carbamyltransferase precursor (pOCT
1-19). When added to an in vitro import assay system, pOCT (1-19) blocked
the import of pOCT specifically: it did not impede the entry and processing
of the precursor to subunit 2 of the F1-ATPase (p beta). This finding
suggests that at least two distinct precursor(s)-specific pathways are
required for the import of mitochondrial inner membrane and matrix
proteins.
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