Journal article
Further investigations regarding the role of trimethyllysine for cytochrome c uptake into mitochondria
International journal of biochemistry, v 23(7), pp 761-768
1991
PMID: 1650724
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
1.
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.
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.
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.
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.
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.
Metrics
Details
- Title
- Further investigations regarding the role of trimethyllysine for cytochrome c uptake into mitochondria
- Creators
- Karamba J CessayLawrence W BergmanMartin T Tuck
- Publication Details
- International journal of biochemistry, v 23(7), pp 761-768
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- [Retired Faculty]
- Web of Science ID
- WOS:A1991FH78000020
- Scopus ID
- 2-s2.0-0025925072
- Other Identifier
- 991014878423804721
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- Web of Science research areas
- Biochemistry & Molecular Biology