Article
Pseudo-wild type revertants from inactive apocytochrome b mutants as a tool for the analysis of the structure/function relationships of the mitochondrial ubiquinol-cytochrome c reductase of Saccharomyces cerevisiae.
The Journal of biological chemistry - 25 Feb 1990
di Rago J P, Netter P, Slonimski P P
Abstract excerpt
We have analyzed the structure/function relationships of the yeast mitochondrial cytochrome b with a new methodology based upon the isolation of pseudo-wild type revertants from well-characterized cytochrome b respiratory deficient mutants. Our goal was to determine how cytochrome b function could be restored in such mutants, at least to some degree, by suppressor mutations within the protein. True wild type...
Topics
- Amino Acid Sequence
- Apoproteins
- Base Sequence
- Cytochrome b Group
- Cytochromes b
- Electron Transport Complex III
- Genes, Fungal
- Intracellular Membranes
- Mitochondria
- Molecular Sequence Data
