Showing papers on "Mitochondrial carrier published in 1973"
TL;DR: In this article, it was shown that yeast aerated in derepression medium containing cycloheximide synthesize the three largest subunit proteins of cytochrome oxidase in the presence of chloramphenicol, an inhibitor of mitochondrial protein synthesis.
123 citations
TL;DR: The results of this study suggest that the 3-β-hydroxysteroid dehydrogenase is present in rat testis mitochondria, free of endoplasmic reticulum and that this enzyme is mainly localized in the inner mitochondrial membrane.
43 citations
TL;DR: The presence in yeast of 80S ribosomal particles attached to the cytoplasmic side of the outer mitochondrial membrane is suggested, suggesting a continuity between endoplasmic reticulum and outer mitochon-like membranes in yeast cells.
Abstract: It is well established that mitochondria possess the ability to synthetize proteins (2, 4, 12, 25) . Recent investigations show that mitochondrial protein synthesis depends, at least in part, on nuclear genes, cytoplasmic ribosomes, and nuclear RNA polymerase (3). Biochemical studies of Kellems and Butow (13) show that 80S cytoplasmic ribosomes (26) bind to purified mitochondria of yeast (13) . These ribosomes differ from intramitochondrial ribosomes (1, 27, 28, 29, 31) by insensitivity to chloramphenicol and sensitivity to cycloheximide . Thus their observations suggest the presence in yeast of 80S ribosomal particles attached to the cytoplasmic side of the outer mitochondrial membrane. A continuity between endoplasmic reticulum and outer mitochondrial membranes has been observed in rat liver and onion stem (17), fungi (5), and Tetrahymena pyriformis (10) ; it was postulated that this continuity played a key role in transferring proteins to the inside of the mitochondria . In yeast cells, however, a continuity between endoplasmic reticulum and outer mitochon-
30 citations
TL;DR: All the protein components of the carrier systems for l-malate, succinate, citrate and alpha-oxoglutarate are coded by nuclear genes and synthesized extramitochondrially by cell-sap ribosomes.
Abstract: 1. Kinetic and equilibrium parameters for the uptake of l-malate, succinate, citrate and α-oxoglutarate by fully functional mitochondria of Saccharomyces cerevisiae were determined. 2. The uptake of l-malate and succinate is mediated by a common carrier, and two other distinct carriers mediate the uptake of citrate and α-oxoglutarate. 3. The properties of the carrier systems for l-malate, succinate and citrate closely resemble those of mammalian mitochondria, but the α-oxoglutarate carrier differs from the mammalian system in minor respects. 4. The composition of the yeast mitochondria was extensively manipulated by (a) anaerobiosis, (b) catabolite repression, (c) inhibition of mitochondrial protein synthesis and (d) elimination of mitochondrial DNA by mutation. 5. The carrier systems for l-malate, succinate, citrate and α-oxoglutarate are essentially similar in the five different types of mitochondria. 6. It is concluded that all the protein components of the carrier systems for l-malate, succinate, citrate and α-oxoglutarate are coded by nuclear genes and synthesized extramitochondrially by cell-sap ribosomes.
29 citations
TL;DR: A protein of molecular weight 29,000 has been isolated from the mitochondrial inner membrane and is a major component of Racker's hydrophobic protein mixture and is also rather selectively released from the inner membrane by lysolecithin treatment.
28 citations
TL;DR: Mitochondria contain all of the machinery known to be required for autonomous translation into protein, of mitochondrial DNA, however, only the RNA components of this machinery are specified by mt-DNA.
10 citations
Journal Article•
1 citations