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A highly basic N‐terminal extension of the mitochondrial matrix enzyme ornithine transcarbamylase from rat liver
Author(s) -
Mclntyre Peter,
Graf Lynda,
Mercer Julian,
Peterson Gregory,
Hudson Peter,
Hoogenraad Nicholas
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80977-1
Subject(s) - ornithine transcarbamylase , mitochondrial matrix , biochemistry , carbamyl phosphate , ornithine carbamoyltransferase , biology , peptide sequence , complementary dna , ornithine , amino acid , histidine , enzyme , microbiology and biotechnology , arginine , urea cycle , gene , cytosol
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.