GroEL-assisted protein folding: does it occur within the chaperonin inner cavity?
The folding of protein molecules in the GroEL inner cavity under the co-chaperonin GroES lid is widely accepted as a crucial event of GroEL-assisted protein folding. This review is focused on the data showing that GroEL-assisted protein folding may proceed out of the complex with the chaperonin. The models of GroEL-assisted protein folding assuming ligand-controlled dissociation of nonnative proteins from the GroEL surface and their folding in the bulk solution are also discussed.
Marchenkov
Victor V
VV
Institute of Protein Research, Russian Academy of Sciences, 142290, Russian Federation, Pushchino, Moscow Region, Institutskaya street, 4, Russia.
Semisotnov
Gennady V
GV
Institute of Protein Research, Russian Academy of Sciences, 142290, Russian Federation, Pushchino, Moscow Region, Institutskaya street, 4, Russia.
D000255:Adenosine Triphosphate / Q000378:metabolism; D001665:Binding Sites; D018835:Chaperonin 10 / Q000378:metabolism / Q000648:ultrastructure; D018834:Chaperonin 60 / Q000378:metabolism* / Q000648:ultrastructure*; D004926:Escherichia coli / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding
D018835:Chaperonin 10; D018834:Chaperonin 60; D000255:Adenosine Triphosphate