Study of the yeast Saccharomyces cerevisiae F1F0-ATPase epsilon-subunit.
The yeast Saccharomyces cerevisiae F1F0-ATPase epsilon-subunit (61 residues) was synthesized by the solid-phase peptide approach under both acidic and basic strategies. Only the latter strategy allowed us to obtain a pure epsilon-subunit. The strong propensity of the protein to produce few soluble dimeric species depending on pH has been proved by size-exclusion chromatography, electrophoresis and mass spectrometry. A circular dichroism study showed that an aqueous solution containing 30% trifluoroethanol or 200 mM sodium dodecyl sulphate is required for helical folding. In both solvents at acidic pH, the epsilon-subunit is soluble and monomeric.
Aznar-Derunes
Céline
C
Unité de Biophysique Structurale, UMR 5471 CNRS, Université Bordeaux 1, Talence, France.
Manigand
Claude
C
Picard
Philippe
P
Dautant
Alain
A
Goetz
Michael
M
Schmitter
Jean-Marie
JM
Precigoux
Gilles
G
D000595:Amino Acid Sequence; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D018360:Crystallography, X-Ray; D019281:Dimerization; D025261:Mitochondrial Proton-Translocating ATPases / Q000737:chemistry*; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D021122:Protein Subunits / Q000737:chemistry; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*; D016415:Sequence Alignment; D017385:Sequence Homology; D012995:Solubility
D021122:Protein Subunits; D029701:Saccharomyces cerevisiae Proteins; D025261:Mitochondrial Proton-Translocating ATPases; C102550:TIM11 protein, S cerevisiae