mit‐ Mutations in the oli2 region of mitochondrial DNA affecting the 20 000 dalton subunit of the mitochondrial ATPase in saccharomyces cerevisiae

Roberts, Henry; Choo, Wan Mee; Murphy, Mark; Marzuki, Sangkot; Lukins, H. B.; Linnane, Anthony W.

doi:10.1016/0014-5793(79)80597-9

Cited by 43 publications

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“…Before the influence of these mutations on the OL12 gene product [4] could be studied by electrophoresis, the identifica- Electrophoresis of mitochondria and immunoprecipitated extracts was carried out on an SDS/acrylamide gel (10-12% gradient, expanded conditions [6]). The gel (seven lanes) was stained by Coomassie blue, dried and radioautographed [6].…”

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confidence: 99%

“…From the mutant at the phol locus, three OLl2-linked revertants were obtained which had an improved but still lowered growth rate. The properties of their respective mitochondrial ATPase were closer to normal, with variations depending on the revertant [6].The OL12 gene product is a peptide of 20 kDa apparent molecular mass [4]. Analyzing this peptide in the phnl mutant and in the revertants we found that it showed modified migration properties on SDS/acrylamide gels.…”

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confidence: 86%

“…The OL12 gene product is a peptide of 20 kDa apparent molecular mass [4]. Analyzing this peptide in the phnl mutant and in the revertants we found that it showed modified migration properties on SDS/acrylamide gels.…”

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confidence: 90%

“…Owing to the leakiness of the phol phenotype (reduced but not nil growth rate on oxidizable carbon sources, 5 -loo% highly oligomycinsensitive ATPase complex, low amounts of OL12 gene product peptides), some translational correction of the frameshift is bound to occur. Based on these results, the compatibility of' abnormal ATPase architecture with modified energetic efficiency is discussed.Some years ago, the phol mutation of Succ.haromyce.s cereiisiae [I] was genetically characterized as belonging to the OLl2 gene on mitochondrial D N A [2, 31, which codes for a ineinbranc component of the mitochondrial ATPase [4]. As expected from this localization, the mitochondrial ATPase produced by a mutant at the p h o l locus exhibited highly abnormal properties: weak membrane linkage, exaggerated activation and dual behaviour on purification.…”

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confidence: 99%

“…Some years ago, the phol mutation of Succ.haromyce.s cereiisiae [I] was genetically characterized as belonging to the OLl2 gene on mitochondrial D N A [2, 31, which codes for a ineinbranc component of the mitochondrial ATPase [4]. As expected from this localization, the mitochondrial ATPase produced by a mutant at the p h o l locus exhibited highly abnormal properties: weak membrane linkage, exaggerated activation and dual behaviour on purification.…”

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The pho1 mutation

Somlo

Clavilier

Dujon

et al. 1985

European Journal of Biochemistry

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The phol mutation belongs to the OL12 gene on mitochondrial DNA of Succharomyces cerevisiue, which codes for a membrane factor subunit of the mitochondrial ATPase (apparent molecular mass 20 kDa). We analysed the ATPase complex from the phol mutant and from three revertants, after immunoprecipitation from mitochondrial extracts, by dodecyl sulphate/acrylamide gel electrophoresis. In two revertants the OL12 gene product appeared as an abundant slower migrating peptide, while in the pho mutant, two bands appeared in very low amounts. For the third revertant, a strong band appeared at the normal level. Sequencing of the OL12 gene from these strains gave the following results: the phol mutation is a frameshift, arising by insertion of an extra thymidine into a group of three. Two of the revertants contain the same group of four thymidines, but genetic compensation of the frameshift occurs 24 base pairs downstream by the loss of four bases, implying a deficit of one codon. The third revertant has recovered the normal three-thymidine sequence. There is excellent correlation between the modified sequences and electrophoretic migration of the peptide product. Owing to the leakiness of the phol phenotype (reduced but not nil growth rate on oxidizable carbon sources, 5 -loo% highly oligomycinsensitive ATPase complex, low amounts of OL12 gene product peptides), some translational correction of the frameshift is bound to occur. Based on these results, the compatibility of' abnormal ATPase architecture with modified energetic efficiency is discussed.Some years ago, the phol mutation of Succ.haromyce.s cereiisiae [I] was genetically characterized as belonging to the OLl2 gene on mitochondrial D N A [2, 31, which codes for a ineinbranc component of the mitochondrial ATPase [4]. As expected from this localization, the mitochondrial ATPase produced by a mutant at the p h o l locus exhibited highly abnormal properties: weak membrane linkage, exaggerated activation and dual behaviour on purification. The cellular growth rate on oxidizable carbon sources, and oxidative phosphorylation in isolated mitochondria, were low but nevertheless measurable. The leaky phenotype and the abnormal properties of the ATPase suggested that there might be a heterogeneous mitochondrial ATPase population in vivo [3, 51. From the mutant at the phol locus, three OLl2-linked revertants were obtained which had an improved but still lowered growth rate. The properties of their respective mitochondrial ATPase were closer to normal, with variations depending on the revertant [6].The OL12 gene product is a peptide of 20 kDa apparent molecular mass [4]. Analyzing this peptide in the phnl mutant and in the revertants we found that it showed modified migration properties on SDS/acrylamide gels. On sequencing the OLl2 gene in these strains, we found that the phol mutation is a frameshift, either compensated or corrected in the revertants. The modified sequences are in excellent correlation with the electrophoretic behaviour of the peptide product. EXPERIMENTAL ...

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Section: Resultsmentioning

confidence: 99%

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confidence: 86%

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confidence: 90%

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confidence: 99%

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confidence: 99%

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