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Amino acid sequence of a new mitochondrially synthesized proteolipid of the ATP synthase of Saccharomyces cerevisiae.

1984; Springer Nature; Volume: 3; Issue: 1 Linguagem: Inglês

10.1002/j.1460-2075.1984.tb01785.x

1460-2075

Jean Velours, Mario Esparza, J Hoppe, Walter Sebald, Bernard Guérin,

ATP Synthase and ATPases Research

Research Article1 January 1984free access Amino acid sequence of a new mitochondrially synthesized proteolipid of the ATP synthase of Saccharomyces cerevisiae. J. Velours J. Velours Search for more papers by this author M. Esparza M. Esparza Search for more papers by this author J. Hoppe J. Hoppe Search for more papers by this author W. Sebald W. Sebald Search for more papers by this author B. Guerin B. Guerin Search for more papers by this author J. Velours J. Velours Search for more papers by this author M. Esparza M. Esparza Search for more papers by this author J. Hoppe J. Hoppe Search for more papers by this author W. Sebald W. Sebald Search for more papers by this author B. Guerin B. Guerin Search for more papers by this author Author Information J. Velours, M. Esparza, J. Hoppe, W. Sebald and B. Guerin The EMBO Journal (1984)3:207-212https://doi.org/10.1002/j.1460-2075.1984.tb01785.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info The purification and the amino acid sequence of a proteolipid translated on ribosomes in yeast mitochondria is reported. This protein, which is a subunit of the ATP synthase, was purified by extraction with chloroform/methanol (2/1) and subsequent chromatography on phosphocellulose and reverse phase h.p.l.c. A mol. wt. of 5500 was estimated by chromatography on Bio-Gel P-30 in 80% formic acid. The complete amino acid sequence of this protein was determined by automated solid phase Edman degradation of the whole protein and of fragments obtained after cleavage with cyanogen bromide. The sequence analysis indicates a length of 48 amino acid residues. The calculated mol. wt. of 5870 corresponds to the value found by gel chromatography. This polypeptide contains three basic residues and no negatively charged side chain. The three basic residues are clustered at the C terminus. The primary structure of this protein is in full agreement with the predicted amino acid sequence of the putative polypeptide encoded by the mitochondrial aap1 gene recently discovered in Saccharomyces cerevisiae. Moreover, this protein shows 50% homology with the amino acid sequence of a putative polypeptide encoded by an unidentified reading frame also discovered near the mitochondrial ATPase subunit 6 gene in Aspergillus nidulans. Previous ArticleNext Article Volume 3Issue 11 January 1984In this issue RelatedDetailsLoading ...