Amino acid substitutions in mitochondrial ATPase subunit 9 of Saccharomyces cerevisiae leading to oligomycin or venturicidin resistance.
A series of isonuclear oligomycin-resistant mutants of Saccharomyces cerevisiae carrying mutations in the mitochondrial oli1 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.
Nagley
P
P
Hall
R M
RM
Ooi
B G
BG
D000595:Amino Acid Sequence; D001483:Base Sequence; D005800:Genes, Fungal; D007783:Lactones / Q000494:pharmacology*; D046911:Macromolecular Substances; D008928:Mitochondria / Q000201:enzymology*; D009840:Oligomycins / Q000494:pharmacology*; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors / Q000235:genetics*; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics; D013329:Structure-Activity Relationship; D014698:Venturicidins / Q000494:pharmacology*
D007783:Lactones; D046911:Macromolecular Substances; D009840:Oligomycins; D014698:Venturicidins; D006180:Proton-Translocating ATPases