Formation of yeast mitochondria.  I.  Kinetics of amino acid incorporation during derepression

Henson, Carl P.; Weber, Celia; Mahler, Henry R.

doi:10.1021/bi00852a040

Cited by 54 publications

(16 citation statements)

References 49 publications

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“…Glucose in appropriate concentration is known to suppress mitochondrial function in yeast (15). When strain K19.10 was cultured in the 2% glucose medium (Na-YEPD), it was sensitive to iodoacetate, an inhibitor of glyceraldehyde 3-phosphate dehydrogenase, and to the reagents DNP and CCCP; the glucose-grown cultures were not affected by cyanide or antimycin ( Table 3).…”

Section: Resultsmentioning

confidence: 99%

Mode of action of yeast toxins: energy requirement for Saccharomyces cerevisiae killer toxin

Skipper¹,

Bussey²

1977

J Bacteriol

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The role of the energy status of the yeast cell in the sensitivity of cultures to two yeast toxins was examined by using 42K release from cells as a measure of toxin action. The Saccharomyces cerevisiae killer toxin bound to sensitive cells in the presence of drugs that interfered with the generation or use of energy, but it was unable to efflux 42K from the cells under these conditions. In direct contrast, the Torulopsis glabrata pool efflux-stimulating toxin induced efflux of the yeast 42K pool was insensitive to the presence of energy poisons in cultures. The results indicate that an energized state, maintained at the expense of adenosine 5'-triphosphate from either glycolytic or mitochondrial reactions, is required for the action of the killer toxin on the yeast cell.

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Section: Resultsmentioning

confidence: 99%

Mode of action of yeast toxins: energy requirement for Saccharomyces cerevisiae killer toxin

Skipper¹,

Bussey²

1977

J Bacteriol

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“…Work from several laboratories has indicated that the great bulk of mitochondrialproteins is synthesized outside the mitochondria (Roodyn & Willde, 1968;Beattie et al, 1967;Henson, Weber, & Mahler, 1968) and transferred into the mitochondrial structure in a subsequent step (Beattie, 1968a;Gonzalez-Cadavid & Campbell, 1967;Kadenbach, 1967). Phospholipid biosynthesis also appears to occur mainly in the endoplasmic reticulum, although several recent reports (Bygrave & Kaiser, 1968;Stoffel & Schiefer, 1968) indicate that the outer mitochondrial membrane fraction may contain the enzymes of phosphofipid biosynthesis.…”

Section: Discussionmentioning

confidence: 99%

The relationship of protein and lipid synthesis during the biogenesis of mitochondrial membranes

Beattie

1969

J. Membrain Biol.

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Rat liver mitochondria were fractionated into inner and outer membrane components at various times after the intravenous injection of(14)C-leucine or(14)C-glycerol. The time curves of protein and lecithin labeling were similar in the intact mitochondria, the outer membrane fraction, and the inner membrane fraction. In rat liver slices also, the kinetics of(3)H-phenylalanine incorporation into mitochondrial KCl-insoluble proteins was identical to that of(14)C-glycerol incorporation into mitochondrial lecithin. These results suggest a simultaneous assembly of protein and lecithin during membrane biogenesisThe proteins and lecithin of the outer membrane were maximally labeledin vivo within 5 min after injection of the radioactive precursors, whereas the insoluble proteins and lecithin of the inner membrane reached a maximum specific acitivity 10 min after injection.Phospholipid incorporation into mitochondria of rat liver slices was not affected when protein synthesis was blocked by cycloheximide, puromycin, or actinomycin D. The injection of cycloheximide 3 to 30 min prior to(14)C-choline did not affect thein vivo incorporation of lecithin into the mitochondrial inner or outer membranes; however treatment with the drug for 60 min prior to(14)C-choline resulted in a decrease in lecithin labeling. These results suggest that phospholipid incorporation into membranes may be regulated by the amount of newly synthesized protein available.When mitochondria and microsomes containing labeled phospholipids were incubated with the opposite unlabeled fractionin vitro, a rapid exchange of phospholipid between the microsomes and the outer membrane occurred. A slight exchange with the inner membrane was observed.

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“…Nevertheless, even this small postincorporation produces a significant elevation over the initial radioactivity immediately after the pulse. It should be noted that, since only 5-15% of mitochondrial protein is intramitochondrially synthesized (Sebald et al, 1968;Henson et al, 1968;Schweyen & Kaudewitz, 1970;Hawley & Greenawalt, 1970;Coote & Work, 1971), most of the label postincorporated would go into mitochondrial components of cytoplasmic origin.…”

Section: Resultsmentioning

confidence: 99%

The lability of the products of mitochondrial protein synthesis in Saccharomyces cerevisiae. A novel method for protein half-life determination

Bakalkin¹,

Kalnov²,

Galkin³

et al. 1978

Biochemical Journal

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A method for the determination of the half-life of mitochondrial translation products in yeast in vivo is proposed. The method uses inhibitors of cytoplasmic and mitochondrial protein synthesis and is based on double-labelling pulse-chase techniques, the second label being used to estimate 'post-incorporation' during the 'chase'. For the first time the difference between post-incroporation and the widely known recycling of the label is considered. These studies show that, in the turnover of mitochondrial translation products, the problem is of post-incorporation into mitochondria (especially from the cell sap) is predominant. The results obtained with this procedure indicate that the half-life of the products of mitochondrial protein synthesis in yeast at the late-exponential phase is about 60 min. The results suggest that mitochondrial transplantation products are subject to proteolysis to acid-soluble forms.

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Formation of yeast mitochondria. I. Kinetics of amino acid incorporation during derepression

Cited by 54 publications

References 49 publications

Mode of action of yeast toxins: energy requirement for Saccharomyces cerevisiae killer toxin

Mode of action of yeast toxins: energy requirement for Saccharomyces cerevisiae killer toxin

The relationship of protein and lipid synthesis during the biogenesis of mitochondrial membranes

The lability of the products of mitochondrial protein synthesis in Saccharomyces cerevisiae. A novel method for protein half-life determination

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