SPECIFIC INTERACTION OF THE ESCHERICHIA-COLI CHAPERONE GROEL (60-KDA HEAT-SHOCK PROTEIN) WITH THE LIGANDED FORM OF THE GALACTOSE BINDING-PROTEIN

The Escherichia coli chaperone GroEL interacts more strongly with the liganded form of the galactose binding protein (the galactose binding protein-galactose complex), than with its unliganded form. This specif ic interaction is reflected by the stimulation of the ATPase activity of GroEL by the liganded galactose binding protein. Interactions betwe en native proteins and chaperones could be more frequent than generall y suspected, and may help to detect protein conformational changes.