Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES.
Pig heart mitochondrial malate dehydrogenase was chemically denatured in guanidine HCl. Upon 50-fold dilution of the denaturant spontaneous refolding could be observed in the temperature range 12-32 degrees C. At 36 degrees C spontaneous refolding was not observed but a stable folding intermediate that is fairly resistant to aggregation was formed. This intermediate is readily refolded by the chaperonins GroEL and GroES and may prove useful in future attempts to describe several aspects of chaperonin action at physiological temperatures.
Peralta
D
D
Department of Biochemistry, La Trobe University, Bundoora, Victoria, Australia.
Hartman
D J
DJ
Hoogenraad
N J
NJ
Høj
P B
PB
D000255:Adenosine Triphosphate / Q000494:pharmacology; D000818:Animals; D001426:Bacterial Proteins / Q000494:pharmacology*; D018835:Chaperonin 10; D018834:Chaperonin 60; D004926:Escherichia coli / Q000737:chemistry; D019791:Guanidine; D006146:Guanidines; D006360:Heat-Shock Proteins / Q000494:pharmacology*; D046911:Macromolecular Substances; D008291:Malate Dehydrogenase / Q000737:chemistry*; D008929:Mitochondria, Heart / Q000201:enzymology*; D011489:Protein Denaturation; D017510:Protein Folding; D013552:Swine; D013696:Temperature
D001426:Bacterial Proteins; D018835:Chaperonin 10; D018834:Chaperonin 60; D006146:Guanidines; D006360:Heat-Shock Proteins; D046911:Macromolecular Substances; D000255:Adenosine Triphosphate; D008291:Malate Dehydrogenase; D019791:Guanidine