To fulfill their tasks they need to be folded into a complicated three-dimensional structure. Scientists from the Max Planck Institute of Biochemistry (MPIB) in Martinsried near Munich, Germany, have now analyzed one of the key players of the folding process: the molecular chaperone DnaK.
The chaperone DnaK binds to new proteins and mediates their folding. Proteins it cannot fold, DnaK transports to GroEL, a highly specialized folding machine. Grafic: F.-Ulrich Hartl / Copyright: MPI of Biochemistry
MPIB scientists have now investigated the organization of this network in the bacterium Escherichia coli. Using proteomic analyses they show how different chaperones cooperate during the folding process. “We identified the Hsp70 protein DnaK as the central player of the network,” explains Ulrich Hartl. “It functions as a kind of turntable.” DnaK binds to about 700 different protein chains as they are synthesized. Furthermore, DnaK mediates the folding of most of these protein chains. Those it cannot fold are transferred to yet another chaperone, the barrel-shaped GroEL. GroEL is a highly specialized folding machine. It forms a nano-cage in which a single protein chain is temporarily enclosed and allowed to fold while protected from external influences.
Anja Konschak | Max-Planck-Institut
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