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Amino acid substitutions in mitochondrial ATPase subunit 9 of saccharomyces cerevisiae leading to oligomycin or venturicidin resistance
Author(s) -
Nagley Phillip,
Hall Ruth M.,
Ooi Beng Guat
Publication year - 1986
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(86)80152-1
Subject(s) - oligomycin , saccharomyces cerevisiae , protein subunit , biology , inner mitochondrial membrane , amino acid , biochemistry , mutant , mitochondrion , mitochondrial dna , gene , peptide sequence , atpase , genetics , enzyme
A series of isonuclear oligomycin‐resistant mutants of Saccharomyces cerevisiae carrying mutations in the mitochondrial olil gene has been studied. DNA sequence analysis of this gene has been used to define the amino acid substitutions in subunit 9 of the mitochondrial ATPase complex. A domain of amino acids involved in oligomycin resistance can be recognized which encompasses residues in each of the two hydrophobic portions of the subunit 9 polypeptide that are thought to span the inner mitochondrial membrane. Certain amino acid substitutions also confer cross‐resistance to venturicidin: these residues define an inner domain for venturicidin resistance. The expression of venturicidin resistance resulting from one particular substitution is modulated by nuclear genetic factors.