Altered mitochondrial ribosomes in a cytoplasmic mutant of yeast

Grivell, Les; Reijnders, L.; Vries, H. de

doi:10.1016/0014-5793(71)80121-7

Cited by 48 publications

(11 citation statements)

References 21 publications

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“…Since in our opinion a characterization of mitochondrial ribosomes is meaningful only when particles which are fully active in protein synthesis in vitro are used, we have endeavoured to set up a procedure to obtain biologically active particles. The activity in poly(U)-directed polyphenylalanine synthesis of rat liver mitochondrial ribosomes obtained by our procedure is of similar magnitude or even higher than that observed by other investigators with mitochondrial ribosomes from lower organisms [2,3]. Our results demonstrate that two kinds of particles, either 80-6 or 55-5 particles present in mitochondrial lysate are able to catalyze protein synthesis in vitro.…”

Section: Sedimentation Pattern Of Mitochondrial and Cytoplasmic Ribossupporting

confidence: 84%

“…was modified by introducing the washing procedure through a 1 M sucrose layer described by Grivell et al [2] but with the omission of NH,Cl. Extraneous material was indeed removed by this step but the mitochondrial ribosomes thus obtained displayed only slight activity.…”

Section: Isolation Of Mitochondria1 and Cytoplasmic Ribosomes And Thementioning

confidence: 99%

“…The purity of ribosomal preparations was also checked by electron microscopy which revealed that the ribosomal preparations were completely free from contamination of membranes (experiments not shown). Preincubation of mitochondria with puromycin before lysis as described by Grivell et al for yeast mitochondria [2] resulted in a loss of catalytic activity. Fig.…”

Section: Isolation Of Mitochondria1 and Cytoplasmic Ribosomes And Thementioning

confidence: 99%

“…They appear to be in the 70-to 80-5 size range, but completely different in physicochemical properties from their cytoplasmic counterparts [l]. The isolated ribosomes in several cases retain in vitro a significant capacity to synthesize proteins [2,3]. On the other hand a complete characterization of mitochondrial ribosomes from animal cells is still lacking.…”

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confidence: 99%

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Isolation and Characterization of Rat‐Liver Mitochondrial Ribosomes Highly Active in Poly(U)‐Directed Polyphenylalanine Synthesis

Greco

Cantatore

Pèpe

et al. 1973

European Journal of Biochemistry

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The procedure used to obtain mitochondrial ribosomes from rat liver highly active in catalyzing a poly(U)-dependent polyphenylalanine synthesis is described.Two kinds of particles with sedimentation coefficients of 80-S and 55-5, present in the mitochondrial lysate, are able to catalyze protein synthesis in vitro.Sensitivity to specific inhibitors of protein synthesis demonstrates that the activity of 55-5 particles is only of niitochondrial origin whereas that of 80-5 particles is partly due to mitochondrial ribosomes and partly to contaminating cytoplasmic ribosomes.Characterization of the two kinds of mitochondrial particles has been carried out by studying their sedimentation pattern in different experimental conditions and by analyzing the RNA extracted by polyacrylamide gel electrophoresis. 16-S and 12-5 RNA seem to be specific mitochondrial ribosomal species.The results suggest that the 56-5 particle represents the basic unit for protein synthesis in rat liver mitochondria. Particles with higher sedimentation value probably represent aggregates of mitochondrial monosomes.

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Section: Sedimentation Pattern Of Mitochondrial and Cytoplasmic Ribossupporting

confidence: 84%

Section: Isolation Of Mitochondria1 and Cytoplasmic Ribosomes And Thementioning

confidence: 99%

Section: Isolation Of Mitochondria1 and Cytoplasmic Ribosomes And Thementioning

confidence: 99%

mentioning

confidence: 99%

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Isolation and Characterization of Rat‐Liver Mitochondrial Ribosomes Highly Active in Poly(U)‐Directed Polyphenylalanine Synthesis

Greco

Cantatore

Pèpe

et al. 1973

European Journal of Biochemistry

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“…The cell populations were maintained at 37°C as monolayer cultures in Eagle minimal essential medium as previously described (8). All cell populations were routinely tested for the presence of mycoplasma contaminants by cultural methods (22), uridine-uracil incorporation (22), and the 4,6-diamidino-2-phenylindole assay (19).…”

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confidence: 99%

Effects of mycoplasma contamination on phenotypic expression of mitochondrial mutants in human cells.

Doersen

Stanbridge

1981

Mol. Cell. Biol.

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HeLa cells sensitive to the mitochondrial protein synthesis inhibitors erythromycin (ERY) and chloramphenicol (CAP) and HeLa variants resistant to the effects of these drugs were purposefully infected with drug-sensitive and -resistant mycoplasma strains. Mycoplasma hyorhinis and the ERY-resistant strain of Mycoplasma orale, MO-ERYr, did not influence the growth of HeLa and ERY-resistant ERY2301 cells in the presence or absence of ERY. M. hyorhinis also did not affect the growth of HeLa and CAP-resistant Cap-2 cells in the presence or absence of CAP. However, both HeLa and Cap-2 cells infected with the CAP-resistant strain of M. hyorhinis, MH-CAPr, were more sensitive to the cytotoxic effect of CAP. This may be due to the glucose dependence of the cells, which was compromised by the increased utilization of glucose by MH-CAPr in these infected cell cultures. In vitro protein synthesis by isolated mitochondria was significantly altered by mycoplasma infection of the various cell lines. A substantial number of mycoplasmas copurified with the mitochondria, resulting in up to a sevenfold increase in the incorporation of [3H]leucine into the trichloroacetic acid-insoluble material. More importantly, the apparent drug sensitivity or resistance of mitochondrial preparations from mycoplasma-infected cells reflected the drug sensitivity or resistance of the contaminating mycoplasmas. These results illustrate the hazards in interpreting mitochondrial protein synthesis data derived from mycoplasma-infected cell lines, particularly putative mitochondrially encoded mutants resistant to inhibitors of mitochondrial protein synthesis.

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Biogenesis of Mitochondria 23. The Biochemical and Genetic Characteristics of Two Different Oligomycin Resistant Mutants of Saccharomyces Cerevisiae Under the Influence of Cytoplasmic Genetic Modification

Mitchell

Bunn

Lukins

et al. 1972

Membrane Structure and Mechanisms of Biological Energy Transduction

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Altered mitochondrial ribosomes in a cytoplasmic mutant of yeast

Cited by 48 publications

References 21 publications

Isolation and Characterization of Rat‐Liver Mitochondrial Ribosomes Highly Active in Poly(U)‐Directed Polyphenylalanine Synthesis

Isolation and Characterization of Rat‐Liver Mitochondrial Ribosomes Highly Active in Poly(U)‐Directed Polyphenylalanine Synthesis

Effects of mycoplasma contamination on phenotypic expression of mitochondrial mutants in human cells.

Biogenesis of Mitochondria 23. The Biochemical and Genetic Characteristics of Two Different Oligomycin Resistant Mutants of Saccharomyces Cerevisiae Under the Influence of Cytoplasmic Genetic Modification

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