Assembly of the mitochondrial membrane system XVI. Modified form of the ATPase proteolipid in oligomycin‐resistant mutants of <i>Saccharomyces cerevisiae</i>

Tzagoloff, Alexander; Akai, Anna; Foury, Françoise

doi:10.1016/0014-5793(76)80154-8

Cited by 152 publications

(26 citation statements)

References 11 publications

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“…Mutations in oli 1 were found to modify certain properties of the yeast proteolipid (137). The localization of alleles conferring the resistance phenotype in the structural gene of the proteolipid has been fully confirmed by protein sequence data (111).…”

Section: Genetic Specification Of the Proteolipidmentioning

confidence: 77%

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Mitochondrial Genes and Translation Products

Tzagoloff¹,

Macino²

1979

Annu. Rev. Biochem.

245

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Section: Genetic Specification Of the Proteolipidmentioning

confidence: 77%

“…There was some earlier evidence that the oli 1 resistance locus is in the structural gene of the proteolipid (137,138). Mutations in oli 1 were found to modify certain properties of the yeast proteolipid (137).…”

Section: Genetic Specification Of the Proteolipidmentioning

confidence: 99%

Mitochondrial Genes and Translation Products

Tzagoloff¹,

Macino²

1979

Annu. Rev. Biochem.

245

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“…Both mutants were derived from the respiratory-competent haploid strain D273-10B/A21 (6). This strain has a mitochondrial genome with the three drug-resistant markers oli1 R , ery R , and par R .…”

Section: Phenotype Of Mutants From Complementation Group G158 -mentioning

confidence: 99%

MTO1 Codes for a Mitochondrial Protein Required for Respiration in Paromomycin-resistant Mutants of Saccharomyces cerevisiae

Colby

Tzagoloff

1998

Journal of Biological Chemistry

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100

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Mutations in MTO1 express a respiratory defect only in the context of a mitochondrial genome with a paromomycin-resistance allele. This phenotype is similar to that described previously for mss1 mutants by Decoster, E., Vassal, A., and Faye, G. (1993) J. Mol. Biol. 232, 79 -88. We present evidence that Mto1p and Mss1p are mitochondrial proteins and that they form a heterodimer complex.In a paromomycin-resistant background, mss1 and mto1 mutants are inefficient in processing the mitochondrial COX1 transcript for subunit 1 of cytochrome oxidase. The mutants also fail to synthesize subunit 1 and show a pleiotropic absence of cytochromes a, a 3 , and b. In vivo pulse labeling of an mto1 mutant, however, indicate increased rates of synthesis of other mitochondrial translation products. The respiratory defective phenotype of mto1 and mss1 mutants is not seen in a paromomycin-sensitive genetic background. The visible absorption spectra of such strains indicate a higher ratio of cytochromes b/a and elevated NADH-and succinate-cytochrome c reductase activities. To explain these phenotypic characteristics, we proposed that the Mto1p⅐Mss1p complex plays a role in optimizing mitochondrial protein synthesis in yeast, possibly by a proofreading mechanism.

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“…It is still unknown whether the high-molecular-weight species represents a polymer or a complex with another component. In certain ATPase mutants the proteolipid was found either to be absent [78] or only to be present in the low-molecular-weight form [79]. The polypeptide from S. cerevisiae has been analysed by Sierra and Tzagoloff [75].…”

Section: Ivd Isolated Hydrophobic Subunitsmentioning

confidence: 99%

“…By in vitro reconstitution experiments in reciprocal systems (F 1, OSCP and membrane factor from either wild-type or mutant) this alteration was found to reside in the membrane factor [103,104]. Recently, the mitochondrially synthesized proteolipid of yeast ATPase was shown to be present only in the low molecular weight form in OLl I mutants isolated independently in different laboratories [79]. The OLl 2 mutants contained the proteolipid in the high-molecularweight form (see also section IVD).…”

Section: Va Cytoplasmic Mutantsmentioning

confidence: 99%