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Molecular analysis of revertants from a respiratory‐deficient mutant affecting the center o domain of cytochrome b in Saccharomyces cerevisiae
Author(s) -
Thierry Tron,
Pascale Infossi,
JeanYves Coppée,
AnneMarie Colson
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80075-e
Subject(s) - mutant , biology , cytochrome b , saccharomyces cerevisiae , mutation , microbiology and biotechnology , cytochrome , oligonucleotide , cytochrome c , gene , chemistry , genetics , biochemistry , mitochondrial dna , mitochondrion , enzyme
In bc complexes, cytochrome b plays a major role in electron transfer and in proton translocation accross the membrane. Several inhibitor‐resistant and respiratory‐deficient mutants have already been used to study the structure‐function relationships of this integral membrane protein. We describe here the selection and the molecular analysis of revertants from a thermo‐sensitive mit‐mutant of known nucleotide changes. Among 80 independent pseudo‐wild type revertants screened by DNA‐labelled oligonucleotide hybridization, 33 have been sequenced. Eight suppressor mutations, affecting a region critical for both the function and the binding of center o inhibitors (end of helix C) were identified. Two of them were found to be more resistant to myxothiazol.