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A product of mitochondrial protein synthesis in rat liver mitochondria, characterized by a low molecular weight (Mr < 10000) and an unusually high hydrophobicity, has been identified as the dicyclohexylcarbodiimide-binding protein and as a peptide of the hydrophobic sector of the mitochondrial ATPase complex. The purified protein still possesses the ability to bind dicyclohexylcarbodiimide. [ABSTRACT FROM AUTHOR]

I. This paper describes some features of the protein synthesis in isolated rat liver mitochondria and reports on the stability of the product of mitochondrial protein synthesis in vitro. 2. Chase experiments performed after a 30-min pulse of [14C]leucine indicated that a large part of the product is degraded to an acid-soluble form (labile product) almost as rapidly as it is terminated and released from the mitoribosome. Only a small proportion of the completed product (between 20 and 40 %)is conversed in acid-insoluble form (stable product). 2. Both labile and stable products have an exceptional degree of hydrophobicity, shown by their marked resistance to acid and alkaline hydrolysis and by their solubility in organic solvents. 4. A 14C-labelled peptide with an apparent molecular weight of 12000-13000, as assessed by gel electrophoresis in the presence of dodecylsulfate, is released after heat treatment of mitoribosomes isolated from mitochondria pulsed with [14C]leucine. [ABSTRACT FROM AUTHOR]

Investigates the kinetic properties and biogenesis of wild-type and mutant human adenine nucleotide carrier proteins (HAncp) in the yeast Saccharomyces cerevisiae. Kinetic properties of the three HAncp for the adenosine diphosphate/adenosite triphosphate exchange; Significance of the protein levels for the reduced yeast growth rescued by HANC.