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Published online before print May 2, 2006, 10.1110/ps.062100606
Protein Science (2006), 15:1270-1276. Published by Cold Spring Harbor Laboratory Press. Copyright © 2006 The Protein Society
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Glu257 in GroEL is a sensor involved in coupling polypeptide substrate binding to stimulation of ATP hydrolysis

Oded Danziger1, Liat Shimon1 and Amnon Horovitz

Department of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel

(RECEIVED January 18, 2006; FINAL REVISION February 24, 2006; ACCEPTED March 6, 2006)

The ATPase activity of many types of molecular chaperones is stimulated by polypeptide substrate binding via molecular mechanisms that are, for the most part, unknown. Here, we report that such stimulation of the ATPase activity of GroEL is abolished when its conserved apical domain residue Glu257 is replaced by alanine. This mutation is also found to convert the ATPase profile of GroEL, a group I chaperonin, into one that is characteristic of group II chaperonins. Steady-state and transient kinetic analysis indicate that both effects are due, at least in part, to a reduction of the affinity of GroEL for ADP. This finding indicates that nonfolded proteins stimulate ATP hydrolysis by accelerating the off-rate of the ADP formed, thereby allowing more rapid cycles of ATP binding and hydrolysis.

Keywords: chaperonins; molecular chaperones; allostery; cooperativity; protein folding


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