The formation of symmetrical GroEL-GroES complexes in the presence of ATP.
The incubation of chaperonins cpn60 (GroEL) and cpn10 (GroES) from E. coli in the presence of Mg-ATP and KCl generates the formation, as revealed by electron microscopy, of GroEL-GroES complexes with a symmetrical shape in which one toroidal GroES oligomer is bound to each end of the tetradecameric GroEL aggregate (1:2 GroEL:GroES oligomer molar ratio). The symmetrical complexes are not observed in the presence of ADP or the non-hydrolyzable ATP analog, ATP gamma S, where only asymmetrical complexes (1:1 GroEL:GroES oligomer molar ratio) are formed. These results suggest that ATP hydrolysis is required for the formation of symmetrical complexes.
Llorca
O
O
Centro Nacional de Biotecnología, CSIC, universidad Autónoma de Madrid, Spain.
Marco
S
S
Carrascosa
J L
JL
Valpuesta
J M
JM
D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D002417:Cattle; D018835:Chaperonin 10; D018834:Chaperonin 60; D004926:Escherichia coli / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D008854:Microscopy, Electron; D011485:Protein Binding; D011489:Protein Denaturation; D017510:Protein Folding; D013884:Thiosulfate Sulfurtransferase / Q000737:chemistry / Q000378:metabolism
D001426:Bacterial Proteins; D018835:Chaperonin 10; D018834:Chaperonin 60; D006360:Heat-Shock Proteins; D000255:Adenosine Triphosphate; D013884:Thiosulfate Sulfurtransferase