期刊论文详细信息
FEBS Letters
Amino acid substitutions in mitochondrial ATP synthase subunit 9 of Saccharomyces cerevisiae leading to venturicidin or ossamycin resistance
Nagley, Phillip2  Galanis, Maria2  Mattoon, James R.1 
[1] Biology Department, University of Colorado, Colorado Springs, CO 80933-7150, USA;Department of Biochemistry and Centre for Molecular Biology and Medicine, Monash University, Clayton, Victoria 3168 Australia
关键词: ATPase complex;    mitochondrial;    Amino acid substitution;    Venturicidin;    Ossamycin;    Drug-resistance domain;    Gene;    oli1;    (Saccharomyces cerevisiae);    mtATPase;    mitochondrial proton-translocating ATP synthase;    mtDNA;    mitochondrial DNA;    venR;    venturicidin-resistant;    ossR;    ossamycin-resistant;    oliR;    oligomycin-resistant (in reference to phenotype);   
DOI  :  10.1016/0014-5793(89)80653-2
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

A series of mitochondrially inherited mutants of yeast has been analysed, which were previously identified as showing resistance to the antibiotics venturicidin or ossamycin and whose mutations showed tight linkage to oligomycin-resistance alleles affecting subunit 9 of the mitochondrial ATP synthase. DNA sequence analysis of the oli1 gene of these mutants has been used to define the nature of amino acid substitution in the subunit 9 protein. In the case of the two venturicidin-resistant mutants, mutations affect amino acids on the N-terminal stem of the protein, namely G1y25 → Ser (venR ossS oliR) and Ala 27 → Gly (venR ossS oliS). The mutations found in the two ossamyein-resistant mutants affect amino acids on the C-terminal stem of the protein, namely Leu53 → Phe (vanS ossR oliR) and Leu57 → Phe (venS OSSR oliS). These results allow us to further develop a fine structure map of domains within the subunit 9 protein involved in antibiotic interaction.

【 授权许可】

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