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Processing of Artificial Peptide-DNA-Conjugates by the Mitochondrial Intermediate Peptidase (MIP)
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M. Seibel
Published/Copyright:
June 1, 2005
Abstract
Import of DNA from the cytoplasm into the mitochondrial matrix is an obligatory step for an in organello site-directed mutagenesis or gene therapy approach on mitochondrial DNA diseases. In this context, we have developed an artificial DNA translocation vector that is composed of the mitochondrial signal peptide of the ornithine transcarbamylase (OTC) and a DNA moiety. While this vector is capable of directing attached passenger molecules to the mitochondrial matrix, the recognition of this artificial molecule by the endogenous mitochondrial signal peptide processing machinery as well as the cleavage of the peptide plays a pivotal role in the release of the attached DNA. To study the proteolytic processing of the artificial vector, various signal peptide-DNA-conjugates were treated with purified mitochondrial intermediate peptidase. When the leader peptide is directly linked to the DNA moiety without an intervening spacer, MIP processing is prevented. Cleavage of the peptide can be restored, however, when the first ten amino acid residues of the mature part of OTC are appended at the carboxy-terminal end of the signal peptide. Our results show that artificial peptide-DNA-conjugates are recognized by the mitochondrial proteolytic machinery, and therefore an interference of the peptide with the DNA function can be excluded.
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Published Online: 2005-06-01
Published in Print: 1999-07-01
Copyright © 1999 by Walter de Gruyter GmbH & Co. KG
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Articles in the same Issue
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- Cyclin Dependent Kinases and Regulation of the Fission Yeast Cell Cycle
- Paper of the Year 1998
- Autonomous Regulation in Mammalian Mitochondrial DNA Transcription
- Prospects for the Precise Engineering of Plant Genomes by Homologous Recombination
- The Glycosphingolipidoses from Disease to Basic Principles of Metabolism
- The Dual Role of Lipopolysaccharide as Effector and Target Molecule
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- Mitochondria Harbouring Mutant mtDNA a Cuckoo in the Nest?
- Mutant p53: Gain-of-Function Oncoproteins and Wild-Type p53 Inactivators
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