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Purification and characterization of a GroEL homologue from the moderately eubacterial halophile Pseudomonas sp. #43
M Tokunaga1, H Miyawaki, Y Shiraishi
1Laboratory of Applied and Molecular Microbiology, Faculty of Agriculture, Kagoshima University, Japan. tokunaga@chem.agri.kagoshima-u.ac.jp
Abstract:
We have purified to apparent homogeneity and characterized a molecular chaperonin GroEL homologue (hpGroEL) from a moderately halophilic eubacterium, Pseudomonas sp. #43. Although this halophilic bacterium requires 1-2 M NaCl for growth, hpGroEL did not require a high concentration of salt for its stability, ATPase activity and refold-promoting activity for denatured protein. The ATPase activity was even more halo-sensitive than that of GroEL from Escherichia coli. The hpGroEL protein promotes Mg(2+)-ATP-dependent refolding of urea-denatured alpha-glucosidase in the presence of E. coli-GroES, indicating that chaperonins 60 and 10 isolated from halophilic and nonhalophilic eubacteria, respectively, can cooperate with each other.