The mitochondrial structural proteins from wild-type and respiratory-deficient yeasts

Katoh, Takahiro; Sanukida, Satoshi

doi:10.1016/0006-291x(65)90204-4

Cited by 17 publications

(4 citation statements)

References 7 publications

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“…The results presented in this communication differ from those obtained by Iiatoh and Sanukida [15] who tested the reaction between SP and anti-SP antisera using immunodiffusion in agar gels and a passive cutaneous anaphylactic reaction and were unable to detect any difference between wSP and pSP. It is evident that the methods employed by these authors were not suited to reveal the subtle antigenic m e rence between the two otherwise very similar protein preparations.…”

Section: Discussioncontrasting

confidence: 99%

“…It was thus reasonable to assume that this change would be reflected in an altered composition of the mitochondrial structural protein. Previous studies, however, which involved amino-acid analyses and immunological methods, failed to detect any difference between the structural protein from mitochondria of wild-type yeast (wSP) and that of a cytoplasmic ("petite colonie") mutant (pSP) [15]. The present work, in contrast, provides electrophoretic and immunological evidence for the absence from pSP of at least one of the components of WSP.…”

Section: 3contrasting

confidence: 80%

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Structural Protein of Wild‐Type (ρ⁺) and Respiration‐Deficient (ρ⁻) Yeast Mitochondria

Tuppy

Swetly

Wolff

1968

European Journal of Biochemistry

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Structural protein prepared from mitochondria of wild-type baker's yeast contains several components which are separable by electrophoresis on polyacrylamide gels. One of these components is absent from structural protein preparations obtained from a cytoplasmic "petite" mutant.Rabbit antisera against the structural protein of yeast mitochondria are capable of agglutinating yeast mitochondria and human erythrocytes coated with yeast mitochondrial structural protein. The agglutination of coated erythrocytes can be inhibited by absorption of antisera with structural protein. With the help of this sensitive haemagglutination-inhibition technique the antigenic properties of structural protein from mitochondria of the wild-type yeast and the "petite" mutant were compared. It was found that at least one of the antigenic determinants present in the mitochondrial structural protein preparations from wild-type yeast is lacking in those obtained from the mutant.Saccharomyces cerevisiae easily undergoes nonchromosomal mutations which result in loss of respiratory capacity. The mutants derive the energy required for growth and reproduction exclusively from fermentation and therefore form small colonies on solid media poor in glucose. The mitochondria of the "petite" mutants differ from normal yeast mitochondria both morphologically and biochemically [1,2]. The respiratory block has been accounted for by a total absence from the mitochondria of cytochrome oxidase and a complete or near complete deficiency in cytochromes b and c1 [3]. Mitochondria1ATPase associated with the "petite" yeast mitochondria is cold-labile and oligomycin-insensitive [4], whereas the same enzyme in wild-type mitochondria is stable to cold and sensitive to oligomycin 151.It is likely that the extrachromosomal genetical factor(s) involved in the petite mutation are located in the mitochondria themselves. Isolated yeast mitochondria, like mitochondria of other organisms, contain a DNA species which differs from chromosomal DNA with respect to base composition, melting behaviour and buoyant density [S-81. Studies on isolated mitochondria have indicated that the endogenous DNA has an important role in mitochondrial RNA and protein synthesis [9,10]. As first shown for Unusual Abbreviations. SP, structural protein of yeast mitochondria ; wSP, structural protein from mitochondria of wild-type yeast; pSP, structural protein from mitochondria of a cytoplasmic ("petite colonie") mutant.Enzyme. ATPase or ATP phosphohydrolase (EC 3.6.1.3). 2.3.isolated rat-liver mitochondria, radioactive aminoacids are incorporated predominantly into an insoluble protein fraction [l I, 121 which resembles mitochondrial "structural protein" [13]. I n contrast, the components of the respiratory chain are only insignificantly labelled. These results suggest that structural protein may be a main product of the mitochondrial genetic system. The "petite" mutation has been shown not to deprive the yeast mitochondria of all of their endogenous DNA but to result in a marked change of its ...

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Section: Discussioncontrasting

confidence: 99%

Section: 3contrasting

confidence: 80%

Structural Protein of Wild‐Type (ρ⁺) and Respiration‐Deficient (ρ⁻) Yeast Mitochondria

Tuppy

Swetly

Wolff

1968

European Journal of Biochemistry

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“…In the ultracentrifuge a solution of the protein prepared by the method of Richardson et al (1964) and dissolved in 0.5% sodium dodecyl sulfate shows a single symmetrical peak although there is some material which sediments very rapidly to the bottom of the cell. The average sedimentation velocity constant of the single peak (three runs) wass20lU = 1.96 ± 0.04 S which compares very closely with the value of s2o,« = 1.95 obtained by Katoh and Sanukida (1965) for yeast mitochondrial structural protein and with the values of Sio.u = 1.9-2.2 found by Criddle et al (1962) for beef heart mitochondrial structural protein and from which they estimated a molecular weight of 22,000 for the monomeric form of the proteins in sodium dodecyl sulfate.…”

Section: Resultssupporting

confidence: 86%

“…Like mitochondrial structural proteins it is insoluble at neutral pH, in 8 m urea at pH 7.2, in 1% Triton X-100 at pH 7.2, but dissolves in 0.1% sodium dodecyl sulfate at pH 7.4 and in alkali in pH 11 (Criddle et al, 1962). It also binds phospholipids and values for the sedimentation velocity coefficient of the main protein component when dissolved in sodium dodecyl sulfate at pH 7.4 are extremely close to values reported for both beef heart and yeast mitochondrial structural protein (Criddle et al, 1962;Katoh and Sanukida, 1965). Like mitochondrial structural protein it is inhomogeneous when dissolved in phenol-acetic acid-2 m urea (MacLennan and Tzagoloff, 1968).…”

supporting

confidence: 61%

Membrane proteins from Bacillus megaterium KM

Mirsky¹

1969

Biochemistry

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Oxidative Phosphorylierung in Mitochondrien

Schatz¹

1967

Angewandte Chemie

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Mitochondrien können aus ADP und anorganischem Phosphat ATP bilden, wobei der Energiebedarf durch die Atmung gedeckt wird. Dieser gekoppelte Prozeß wird als oxidative Phosphorylierung bezeichnet. In ausreichend mit Sauerstoff versorgten normalen tierischen Zellen wird auf diese Weise die Hauptmenge an ATP synthetisiert. Der Mechanismus der oxidativen Phosphorylierung ist unbekannt. Der Ablauf der Gesamtreaktion ist eng an die innere Mitochondrienmembran gebunden. Als erstes läßt sich ein energiereiches Primärprodukt nachweisen, das in noch unbekannter Weise ATP bildet. An der Kopplung von Atmung und ATP‐Synthese sind Proteine der inneren Mitochondrienmembran beteiligt, die als „Kopplungsfaktoren”︁ bezeichnet werden. Der Verlauf der oxidativen Phosphorylierung wird zur Zeit an drei Hypothesen diskutiert: der „chemischen”︁, der „chemiosmotischen”︁ und der „Konformationshypothese”︁. Eine Entscheidung zwischen diesen Hypothesen ist noch nicht möglich.

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The mitochondrial structural proteins from wild-type and respiratory-deficient yeasts

Cited by 17 publications

References 7 publications

Structural Protein of Wild‐Type (ρ⁺) and Respiration‐Deficient (ρ⁻) Yeast Mitochondria

Structural Protein of Wild‐Type (ρ⁺) and Respiration‐Deficient (ρ⁻) Yeast Mitochondria

Membrane proteins from Bacillus megaterium KM

Oxidative Phosphorylierung in Mitochondrien

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The mitochondrial structural proteins from wild-type and respiratory-deficient yeasts

Cited by 17 publications

References 7 publications

Structural Protein of Wild‐Type (ρ+) and Respiration‐Deficient (ρ−) Yeast Mitochondria

Structural Protein of Wild‐Type (ρ+) and Respiration‐Deficient (ρ−) Yeast Mitochondria

Membrane proteins from Bacillus megaterium KM

Oxidative Phosphorylierung in Mitochondrien

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Product

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Structural Protein of Wild‐Type (ρ⁺) and Respiration‐Deficient (ρ⁻) Yeast Mitochondria

Structural Protein of Wild‐Type (ρ⁺) and Respiration‐Deficient (ρ⁻) Yeast Mitochondria