Relationship between a stress membrane protein of Oenococcus oeni and glyceraldehyde-3-phosphate dehydrogenases.
The goal of this study was to analyze how the profiles of membrane proteins of Oenococcus oeni change under particular stress conditions of wine. Sodium dodecyl sulfate polyacrylamide gel electrophoresis protein profiles of membrane fraction showed that a 40-kDa protein was overexpressed in the presence of SO2. The sequence of its N-terminal fragment showed a significant identity with glyceraldehyde-3-phosphate dehydrogenases (GAPDHs), but the protein showed no GAPDH activity. This sequence was compared with those of other GAPDHs with ClustalW alignment, and it was found to be somewhat similar to that of the cell-wall and membrane proteins of other lactic acid bacteria.
Carreté
Ramon
R
Departament de Bioquímica i Biotecnologia, Unitat d'Enologia del CeRTA, Universitat Rovira i Virgili, Campus Sescelades, C. Marcel.lí Domingo s/n 43007, Tarragona, Catalonia, Spain.
Reguant
Cristina
C
Bordons
Albert
A
Constantí
Magda
M
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000032:analysis* / Q000096:biosynthesis; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000032:analysis* / Q000096:biosynthesis; D007777:Lactobacillaceae / Q000201:enzymology* / Q000254:growth & development; D008565:Membrane Proteins / Q000032:analysis* / Q000096:biosynthesis; D008969:Molecular Sequence Data; D020539:Sequence Analysis, Protein / Q000379:methods; D014920:Wine / Q000382:microbiology
D001426:Bacterial Proteins; D008565:Membrane Proteins; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases