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Mitochondrial ATPase : biochemical and molecular genetic analysis
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Bowman, Sharen (1989) Mitochondrial ATPase : biochemical and molecular genetic analysis. PhD thesis, University of Warwick.
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Official URL: http://webcat.warwick.ac.uk/record=b3202751~S15
Abstract
S.cerevisiae mutants were isolated showing nuclear-coded resistance to the antibiotic venturicidin, a known F₀ATPase binding antibiotic. Two types of mutant were identified, one of which had cross-resistance to a variety of antibiotics and appeared linked to the leu₁ locus on chromosome VII, and one which was cross-resistant to chloramphenicol only and not linked to leu₁. The level of resistance to venturicidin was not increased in isolated mitochondria, therefore resistance shown in both groups is believed to be due to a decrease in plasma membrane permeability to these antibiotics.
The fluorescence properties of several organotin compounds, derivatives of the substituted flavones 3-hydroxyflavone (hof) and penta-hydroxyflavone (morin), were investigated on incubation with rat liver mitochondria. The compound Bu₂SnBr(of) was found to show fluorescence enhancement when added to mitochondrial preparations, which could be lowered by addition of the non-fluorescent compound Bu3SnAc. Addition of Bu₂SnBr(of) did not affect mitochondrial membrane potential, and conversely the energetic state of the mitochondrial inner membrane had no effect on Bu₂SnBr(of) fluorescence. This compound was shown to be an inhibitor of mitochondrial ATPase, and is thought to have its binding site on the F₀ moiety of that enzyme complex.
The nuclear gene causing respiratory deficiency in the complementation group G57 was cloned and sequenced. This gene (PET₅₇) encoded a protein of 36 Kdal which did not show significant homology with any known protein. The mutant strain was deficient in mitochondrial ATPase activity, but the major F₁ATPase subunits were detected in mutant mitochondria, although in reduced amounts. Mutant F₁ showed abnormal membrane binding and could not be isolated by standard methods. The protein encoded by the gene PET₅₇ is transported into mitochondria and is thought to contribute to processing or assembly of one or more of the cytoplasmic subunits of the F₁F₀ATPase complex.
Item Type: | Thesis (PhD) | ||||
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Subjects: | Q Science > QD Chemistry | ||||
Library of Congress Subject Headings (LCSH): | Adenosine triphosphatase, Mitochondria, Saccharomyces cerevisiae, Drug resistance in microorganisms | ||||
Official Date: | April 1989 | ||||
Dates: |
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Institution: | University of Warwick | ||||
Theses Department: | Department of Chemistry | ||||
Thesis Type: | PhD | ||||
Publication Status: | Unpublished | ||||
Supervisor(s)/Advisor: | Walbridge, M. G. H. ; Tzagoloff, Alexander, 1937- | ||||
Sponsors: | Science and Engineering Research Council (Great Britain) | ||||
Format of File: | |||||
Extent: | xiii, 180 leaves : illustrations, charts | ||||
Language: | eng |
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