@article {485,
	title = {A novel extranuclear mutant of Neurospora with a temperature-sensitive defect in mitochondrial protein synthesis and mitochondrial ATPase.},
	journal = {Mol Gen Genet},
	volume = {181},
	number = {1},
	year = {1981},
	month = {1981},
	pages = {13-9},
	abstract = {[C93] is a novel, extranuclear mutant of Neurospora crassa which has a normal mitochondrial phenotype when grown at 25 degrees, but which is deficient in cytochromes b and aa3 when grown at 37 degrees (Pittenger and West 1979). In the present work, the phenotype of [C93] was characterized in greater detail. When [C93] is grown at 37 degrees, the rate of mitochondrial protein synthesis is decreased to approximately 25\% that of wild type; the ratio of mitochondrial small to large ribosomal subunits is decreased to 1:4 and mitochondrial small subunits are deficient in the mitochondrially-synthesized protein, S-5. The mitochondrial ribosome assembly defects in 37 degrees-grown [C93] resemble those in chloramphenicol-treated wild-type cells and could merely be a consequence of the decreased rate of mitochondrial protein synthesis. Analysis of mitochondrial translation products by SDS gel electrophoresis suggests that 37 degrees-grown [C93] is grossly deficient in the 19,000 Mr subunit of the oligomycin-sensitive ATPase relative to other mitochondrially-synthesized proteins. The ATPase defect was not found in other extranuclear or nuclear mutants deficient in mitochondrial protein synthesis. These data and additional evidence suggest that the primary defect in [C93] may be in the assembly of the ATPase complex. The possible connection between the ATPase defect and the deficiency of mitochondrial protein synthesis is discussed.},
	keywords = {Adenosine Triphosphatases, Cytochrome b Group, Cytochromes, Electron Transport Complex IV, Electrophoresis, Polyacrylamide Gel, Fungal Proteins, Mitochondria, Mutation, Neurospora, Neurospora crassa, Oligomycins, Ribosomes, Temperature},
	issn = {0026-8925},
	author = {Collins, R A and Bertrand, H and Lapolla, R J and Lambowitz, A M}
}
