Isolation and characterization of a mitochondrially synthesized polypeptide from Neurospora crassa cni-1 mutant.
A polypeptide with a molecular weight of 8 500 (HP 8 500) was isolated from the mitochondrial membrane of the nuclear mutant cni-1 of Neurospora crassa. This mutant is characterized by a cyanide-insensitive respiration and by a deficiency in the cytochromes aa3 and b. The polypeptide is synthesized on mitochondrial ribosomes. It has an extremely hydrophobic character; it is insoluble in aqueous media in the absence of sodium dodecylsulfate and is soluble in acid chloroform/methanol. It lacks histidine. The polar amino acids lysine, arginine, aspartic acid, glutamic acid, serine and threonine make up only 25% of the total amino acids on a mole-percent basis. The N-terminal amino acid is tyrosine. The possible function of this polypeptide in the mitochondrial membrane is discussed.
D002467:Cell Nucleus / Q000378:metabolism; D003486:Cyanides / Q000494:pharmacology; D003513:Cycloheximide / Q000494:pharmacology; D004352:Drug Resistance, Microbial; D008566:Membranes / Q000378:metabolism; D008928:Mitochondria / Q000187:drug effects / Q000378:metabolism*; D008970:Molecular Weight; D009154:Mutation; D009491:Neurospora / Q000378:metabolism*; D009492:Neurospora crassa / Q000187:drug effects / Q000378:metabolism*; D010101:Oxygen Consumption / Q000187:drug effects; D010452:Peptide Biosynthesis; D014176:Protein Biosynthesis
D003486:Cyanides; D003513:Cycloheximide