Insight into topological and functional relationships of cytochrome c oxidase subunit I of Saccharomyces cerevisiae by means of intragenic complementation.
In yeast, revertants were selected from four respiratory deficient mutants carrying mutations in the cytochrome c oxidase subunit I gene. Intragenic second site mutations revealed amino acids which are functionally complementary to the original mutated position and may be in topological interaction with it. The results provide additional data in favour of the model proposed for the structure of the binuclear centre in proton-motive oxidases.
Université Catholique de Louvain, Laboratoire de Génétique Microbienne, Louvain-la-Neuve, Belgium.
B
B
Meunier
F
F
Coster
P
P
Lemarre
A M
AM
Colson
D000595:Amino Acid Sequence; D001483:Base Sequence; D003062:Codon / Q000235:genetics; D003576:Electron Transport Complex IV / Q000737:chemistry* / Q000378:metabolism*; D005800:Genes, Fungal; D005816:Genetic Complementation Test; D007438:Introns; D046911:Macromolecular Substances; D008961:Models, Structural; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D017433:Protein Structure, Secondary; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics
D003062:Codon; D046911:Macromolecular Substances; D003576:Electron Transport Complex IV