A highly basic N-terminal extension of the mitochondrial matrix enzyme ornithine transcarbamylase from rat liver.
We have deduced the amino acid sequence of the N-terminal leader peptide of the mitochondrial enzyme ornithine transcarbamylase from a cDNA clone obtained from a rat liver cDNA library. The sequence is remarkable in being highly basic, having 4 arginine, 3 lysine and 1 histidine with no acidic residues in a total of 32 residues. The leader sequence has no extensive hydrophobic stretches, has 72% homology with the leader peptide of human ornithine transcarbamylase [1], and in terms of its basic character resembles the N-terminal extensions on a number of fungal mitochondrial [2-5] and pea chloroplast [6] proteins. Thus the basic nature of these leader peptides may constitute the signal for mitochondrial import.
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D004247:DNA / Q000032:analysis; D008930:Mitochondria, Liver / Q000201:enzymology*; D009693:Nucleic Acid Hybridization; D009954:Ornithine Carbamoyltransferase / Q000032:analysis*; D012333:RNA, Messenger / Q000032:analysis; D051381:Rats
D012333:RNA, Messenger; D004247:DNA; D009954:Ornithine Carbamoyltransferase