Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate.
Folding of two monomeric enzymes mediated by groE has been reconstituted in vitro. The groEL protein stabilizes the polypeptides in a conformation resembling the 'molten globule' state. Mg-ATP and groES then promote the acquisition of ordered tertiary structure at the surface of groEL. Folding requires the hydrolysis of about 100 ATP molecules per protein monomer. This active process of surface-mediated chain folding might represent a general mechanism for the formation of protein structure in vivo.
Martin
J
J
Institut für Physiologische Chemie Universität München, Germany.
Langer
T
T
Boteva
R
R
Schramel
A
A
Horwich
A L
AL
Hartl
F U
FU
D000255:Adenosine Triphosphate / Q000378:metabolism; D001426:Bacterial Proteins / Q000494:pharmacology*; D018834:Chaperonin 60; D006360:Heat-Shock Proteins / Q000494:pharmacology*; D006868:Hydrolysis; D011487:Protein Conformation / Q000187:drug effects*; D013762:Tetrahydrofolate Dehydrogenase / Q000737:chemistry; D013884:Thiosulfate Sulfurtransferase / Q000737:chemistry
D001426:Bacterial Proteins; D018834:Chaperonin 60; D006360:Heat-Shock Proteins; D000255:Adenosine Triphosphate; D013762:Tetrahydrofolate Dehydrogenase; D013884:Thiosulfate Sulfurtransferase