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Mitochondria of yeast

Achleitner G, Gaigg B, Krasser A, Kainersdorfer E, Kohlwein SD, Perktold A, Zellnig G, Daum G (1999) Association between the endoplasmic reticulum and mitochondria of yeast facilitates interorganelle transport of phospholipids through membrane contact. Eur J Biochem 264 545-553... [Pg.195]

Wintersberger, E. Isolation of a distinct rifampicin-resistant RNA polymerase from mitochondria of yeast, neurospora and liver. Biochem. Biophys. Res. Comm. 48, 1287 (1972)... [Pg.48]

Effect of valinomycin on the respiration and transport of potassium ions in the mitochondria of yeast fungi... [Pg.188]

Figure 8.27. Stereo view of ATP synthase from the mitochondria of yeast, neutral residues in light gray, aromatics in black, other hydrophobics in gray, and charged residues in white. (A) A largely complete ATP synthase double rotary motor Fo-motor, connecting rotor and Fi-motor, with only part of protein... Figure 8.27. Stereo view of ATP synthase from the mitochondria of yeast, neutral residues in light gray, aromatics in black, other hydrophobics in gray, and charged residues in white. (A) A largely complete ATP synthase double rotary motor Fo-motor, connecting rotor and Fi-motor, with only part of protein...
PEP carboxylase occurs in yeast, bacteria, and higher plants, but not in animals. The enzyme is specifically inhibited by aspartate, which is produced by transamination of oxaloacetate. Thus, organisms utilizing this enzyme control aspartate production by regulation of PEP carboxylase. Malic enzyme is found in the cytosol or mitochondria of many animal and plant ceils and is an NADPIT-dependent enzyme. [Pg.665]

Geissler A et al. (2002) The mitochondrial presequence translocase an essential role of Tim50 in directing preproteins to the import channel. Cell 111 507-518 Geli V, Yang MJ, Suda K, Lustig A, Schatz G (1990) The MAS-encoded processing protease of yeast mitochondria. Overproduction and characterization of its two nonidentical subunits. J Biol Chem 265 19216-19222... [Pg.65]

Ferrochelatase (protoheme ferro-lyase)401 403 inserts Fe2+ into protoporphyrin IX to form heme. The enzyme is found firmly bound to the inner membrane of mitochondria of animal cells, chloroplasts of plants, and chromatophores of bacteria. While Fe2+ is apparently the only metallic ion ordinarily inserted into a porphyrin, the Zn2+ protoporphyrin chelate accumulates in substantial amounts in yeast, and Cu2+-heme complexes are known (p. 843). Ferrochelatase, whose activity is stimulated by Ca2+, appears to be inhibited by lead ions, a fact that may account for some of the acute toxicity of lead.404... [Pg.1402]

Not all hereditary traits follow the Mendelian patterns expected for chromosomal genes. Some are inherited directly from the maternal cell because their genes are carried in the cytoplasm rather than the nucleus. There are three known locations for cytoplasmic genes the mitochondria, the chloroplasts, and certain other membrane-associated sites.285 286 An example of the last is found in "killer" strains of yeast. Cells with the killer trait release a toxin that kills sensitive cells but are themselves immune. The genes are carried in double-stranded RNA rather than DNA, but are otherwise somewhat analogous to the colicin factors of enteric bacteria (Box 8-D). Similar particles (kfactors) are found in Paramecium.287... [Pg.1507]


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See also in sourсe #XX -- [ Pg.6 ]

See also in sourсe #XX -- [ Pg.227 , Pg.228 ]

See also in sourсe #XX -- [ Pg.6 ]




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