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A highly basic N-terminal extension of the mitochondrial matrix enzyme ornithine transcarbamylase from rat liver.

Authors
  • McIntyre, P
  • Graf, L
  • Mercer, J
  • Peterson, G
  • Hudson, P
  • Hoogenraad, N
Type
Published Article
Journal
FEBS Letters
Publisher
Wiley (John Wiley & Sons)
Publication Date
Nov 05, 1984
Volume
177
Issue
1
Pages
41–46
Identifiers
PMID: 6548714
Source
Medline
License
Unknown

Abstract

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.

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