The yeast ATP synthase subunit 4: structure and function
| Autor: | Pascal Durrens, Monique Galante, Geneviève Arselin, Bernard Guerin, Jean Velours, Marie-Françoise Paul, Michel Aigle |
|---|---|
| Rok vydání: | 1989 |
| Předmět: |
Protein subunit
Specificity factor Molecular Sequence Data Gi alpha subunit Saccharomyces cerevisiae Biochemistry Gamma-aminobutyric acid receptor subunit alpha-1 Electron Transport Complex IV Structure-Activity Relationship ATP synthase gamma subunit Escherichia coli Animals Eukaryotic Small Ribosomal Subunit Amino Acid Sequence Base Sequence ATP synthase biology Eukaryotic Large Ribosomal Subunit General Medicine Molecular biology Mitochondria Proton-Translocating ATPases Phenotype Mutation biology.protein Nucleic Acid Conformation Cattle Oligonucleotide Probes |
| Zdroj: | Biochimie. 71:903-915 |
| ISSN: | 0300-9084 |
| DOI: | 10.1016/0300-9084(89)90073-4 |
| Popis: | The structure of ATP synthase subunit 4 was determined by using the oligonucleotide probe procedure. This subunit is the fourth polypeptide of the complex when classifying subunits in order of decreasing molecular mass. Its relative molecular mass is 25 kDa. The ATP4 gene was isolated and sequenced. The nucleotide sequence predicts that subunit 4 is probably derived from a precursor protein 244 amino acids long. Mature subunit 4 contains 209 amino acid residues and the predicted molecular mass is 23250 kDa. Subunit 4 shows homology with the b-subunit of Escherichia coli ATP synthase and the b-subunit of beef heart mitochondrial ATP synthase. By using homologous transformation, a mutant lacking wild subunit 4 was constructed. This mutant is devoid of oxidative phosphorylation and F1 is loosely bound to the membrane. Our data are in favor of a structural relationship between subunit 4 and the mitochondrially-translated subunit 6 during biogenesis of F0. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|