Co-expression of plastid chaperonin genes and a synthetic plant Rubisco operon in Escherichia coli.

It has been suggested that lack of specialized molecular chaperone function(s) in Escherichia coli may account for the fact that although E. coli cells transformed with plant Rubisco genes synthesize the Rubisco subunit polypeptides, the active enzyme fails to assemble. If so, co-expression of plant chaperone and Rubisco genes might permit plant Rubisco assembly in E. coli. Introduction of genes encoding plant chaperonin polypeptides has been shown to enhance the capacity of E. coli to assemble active cyanobacterial Rubisco. We now report that co-expression 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.