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Further investigations regarding the role of trimethyllysine for cytochrome c uptake into mitochondria.

Authors
  • Cessay, K J
  • Bergman, L W
  • Tuck, M T
Type
Published Article
Journal
International Journal of Biochemistry
Publisher
Elsevier
Publication Date
Jan 01, 1991
Volume
23
Issue
7-8
Pages
761–768
Identifiers
PMID: 1650724
Source
Medline
License
Unknown

Abstract

1. A mutant of the iso-1-cytochrome c gene from Saccharomyces cerevisiae has been constructed which contains an Arg codon, replacing the normal trimethylated Lys at position 77. 2. This mutated gene was cloned into a pGem 1 vector and used for the in vitro translation of yeast iso-1-cytochrome c. 3. Utilizing an in vitro mitochondria binding assay, it was found that the mutant cytochrome c could transverse the yeast mitochondrial membrane, however the amount of protein incorporated was 3-fold less that of the trimethylated wild type. 4. Omission of the protein methyltransferase from assays containing the wild type cytochrome c caused only a slight reduction (15%) in the amount of protein incorporated. 5. These results suggest while the lysine residue 77 of apocytochrome c is important for mitochondria uptake, the methylation of this residue seems to play a relatively minor role.

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