COEXPRESSION OF PLASTID CHAPERONIN GENES AND A SYNTHETIC PLANT RUBISCO OPERON IN ESCHERICHIA-COLI

It has been suggested that lack of specialized molecular chaperone fun ction(s) in Escherichia coli may account for the fact that although E. coli cells transformed with plant Rubisco genes synthesize the Rubisc o subunit polypeptides, the active enzyme fails to assemble. If so, co -expression of plant chaperone and Rubisco genes might permit plant Ru bisco assembly in E. coli. Introduction of genes encoding plant chaper onin polypeptides has been shown to enhance the capacity of E. coli to assemble active cyanobacterial Rubisco. We now report that co-express ion of plant Rubisco and chaperonin genes affected the solubility and stability of Rubisco large subunit polypeptides, however, neither the assembled oligomeric protein nor Rubisco enzyme activity was detected.