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

FEBS Letters

Hudson, Peter¹  Mclntyre, Peter²  Mercer, Julian³  Graf, Lynda²  Peterson, Gregory³  Hoogenraad, Nicholas¹ 

[1] CSIRO, Division of Protein Chemistry, Parkville, Victoria 3052, Australia;Department of Biochemistry, La Trobe University, Bundoora, Victoria 3083, Australia;Birth Defects Research Institute, Royal Children's Hospital, Parkville, Victoria 3052, Australia

关键词: Mitochondrial import;    Leader sequence;    Urea cycle;    OTC;    ornithine transcarbamylase (EC 2.1.3.3);    pOTC;    precursor form of OTC;    cDNA;    DNA complementary to RNA;    kb;    kilobases;    bp;    base pairs;   

DOI  :  10.1016/0014-5793(84)80977-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown