A highly basic N-terminal extension of the mitochondrial matrix enzyme ornithine transcarbamylase from rat liver |
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Authors: | P McIntyre L Graf J Mercer G Peterson P Hudson N Hoogenraad |
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Institution: | 1. Department of Biochemistry, La Trobe University, Bundoora, Victoria 3083, Australia;2. Birth Defects Research Institute, Royal Children''s Hospital, Parkville, Victoria 3052, Australia;3. CSIRO, Division of Protein Chemistry, Parkville, Victoria 3052, Australia |
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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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Keywords: | 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 |
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