Streptomyces lividanspossesses a GroEL-like chaperonin

Streptomyces lividans grown at 45°C produces a GroEL-like chaperonin. This protein is specifically synthesized in bacterial cell cultures upon heat shock induction. It has a similar size (62 kDa) to the GroEL-like proteins from Eschirichia coli and Bacillus subtilus and shows immunological cross-reaction with serum raised against GroEL like from E. coli. The S. lividans 62-kDa protein assembles into oligomers around 20S that show a morphology consistent with a barrel showing six-fold and seven-fold symmetrues as previously described in E. coli and B. subtilis.