Grape in vivo Protein Synthesis: Changes in Response to Anaerobiosis

Abstract

Protein synthesis was examined in vivo in grape cell culture and ripe berries. Synthesized polypeptides from cell culture and from berries were labeled by ³⁵S-methionine. Protein fractions were analyzed by fluorography of sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Ripe berries were able to synthesize a full set of proteins. Further, transfer from air to anaerobic conditions resulted in qualitative and quantitative changes in polypeptide composition: labeling in certain proteins was constant, while others were labeled to lesser or greater extent during stress. Two-dimensional electrophoresis (IEF-SDS-PAGE) afforded greater resolution of the total polypeptides, describing common features between grape cell culture and berries, and confirming modification upon anaerobiosis in the in vivo protein pattern by increasing synthesis of some polypeptides. We obtained evidence that some of these polypeptides were common in the two models, and that common features between in vivo and in vitro protein synthesis occurred.