Purification and characterization of a GroEL homologue from the moderately eubacterial halophile Pseudomonas sp. #43.
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.
Tokunaga
M
M
Laboratory of Applied and Molecular Microbiology, Faculty of Agriculture, Kagoshima University, Japan. tokunaga@chem.agri.kagoshima-u.ac.jp
Miyawaki
H
H
Shiraishi
Y
Y
Tokunaga
H
H
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D018835:Chaperonin 10 / Q000378:metabolism; D018834:Chaperonin 60 / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D004926:Escherichia coli / Q000737:chemistry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011189:Potassium Chloride / Q000494:pharmacology; D017510:Protein Folding; D011549:Pseudomonas / Q000737:chemistry* / Q000187:drug effects / Q000254:growth & development; D016415:Sequence Alignment; D012965:Sodium Chloride / Q000494:pharmacology; D000520:alpha-Glucosidases / Q000737:chemistry
D018835:Chaperonin 10; D018834:Chaperonin 60; D012965:Sodium Chloride; D011189:Potassium Chloride; D000255:Adenosine Triphosphate; D000520:alpha-Glucosidases; D000251:Adenosine Triphosphatases