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 specific interaction is reflected by the stimulation of the ATPase activity of GroEL by the liganded galactose binding protein. Interactions between native proteins and chaperones could be more frequent than generally suspected, and may help to detect protein conformational changes.
Richarme
G
G
Institut Jacques Monod, Université Paris 7, France.
el Yaagoubi
A
A
de Crouy-Chanel
A
A
Kohiyama
M
M
D000251:Adenosine Triphosphatases / Q000378:metabolism; D002135:Calcium-Binding Proteins; D002352:Carrier Proteins / Q000378:metabolism*; D018834:Chaperonin 60 / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D005690:Galactose / Q000378:metabolism*; D008024:Ligands; D009004:Monosaccharide Transport Proteins; D033902:Periplasmic Binding Proteins; D011485:Protein Binding; D013268:Stimulation, Chemical
D002135:Calcium-Binding Proteins; D002352:Carrier Proteins; D018834:Chaperonin 60; D008024:Ligands; D009004:Monosaccharide Transport Proteins; D033902:Periplasmic Binding Proteins; C023550:galactose-binding protein; D000251:Adenosine Triphosphatases; D005690:Galactose