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A nuclear mutation prevents processing of a mitochondrially encoded membrane protein in Saccharomyces cerevisiae.

1983; Springer Nature; Volume: 2; Issue: 7 Linguagem: Inglês

10.1002/j.1460-2075.1983.tb01544.x

1460-2075

Elke Pratje, Gertrud Mannhaupt, Georg Michaelis, Konrad Beyreuther,

ATP Synthase and ATPases Research

Research Article1 July 1983free access A nuclear mutation prevents processing of a mitochondrially encoded membrane protein in Saccharomyces cerevisiae. E. Pratje E. Pratje Search for more papers by this author G. Mannhaupt G. Mannhaupt Search for more papers by this author G. Michaelis G. Michaelis Search for more papers by this author K. Beyreuther K. Beyreuther Search for more papers by this author E. Pratje E. Pratje Search for more papers by this author G. Mannhaupt G. Mannhaupt Search for more papers by this author G. Michaelis G. Michaelis Search for more papers by this author K. Beyreuther K. Beyreuther Search for more papers by this author Author Information E. Pratje, G. Mannhaupt, G. Michaelis and K. Beyreuther The EMBO Journal (1983)2:1049-1054https://doi.org/10.1002/j.1460-2075.1983.tb01544.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Subunit II of cytochrome oxidase is encoded by the mitochondrial OXI1 gene in Saccharomyces cerevisiae. The temperature-sensitive nuclear pet mutant ts2858 has an apparent higher mol. wt. subunit II when analyzed on lithium dodecylsulfate (LiDS) polyacrylamide gels. However, on LiDS-6M urea gels the apparent mol. wt. of the wild-type protein exceeds that of the mutant. Partial revertants of mutant ts2858 that produce both the wild-type and mutant form of subunit II were isolated. The two forms of subunit II differ at the N-terminal part of the molecule as shown by constructing and analyzing nuclear ts2858 and mitochondrial chain termination double mutants. The presence of the primary translation product in the mutant and of the processed form in the wild-type lacking 15 amino-terminal residues was demonstrated by radiolabel protein sequencing. Comparison of the known DNA sequence with the partial protein sequence obtained reveals that six of the 15 residues are hydrophilic and, unlike most signal sequences, this transient sequence does not contain extended hydrophobic parts. The nuclear mutation ts2858 preventing post-translational processing of cytochrome oxidase subunit II lies either in the gene for a protease or an enzyme regulating a protease. Previous ArticleNext Article Volume 2Issue 71 July 1983In this issue RelatedDetailsLoading ...