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J Biol Chem, Vol. 274, Issue 30, 20756-20758, July 23, 1999

COMMUNICATION
Interaction of 4,4'-Dithiodipyridine with Cys⁴⁵⁸ Triggers Disassembly of GroEL

Elena Bochkareva, Mark Safro^§, and Alexander Girshovich

From the Departments of  Biological Chemistry and ^§ Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel

Chaperonin GroEL, consisting of two seven-subunit rings stacked back-to-back, is disassembled by interaction of 4,4'-dithiodipyridine (DTP) with Cys⁴⁵⁸ located close to the intersubunit contacts within and between the rings. The thiol group of Cys⁴⁵⁸ is inaccessible to the probe being buried into the pocket locked by segment Asn⁴⁷⁵-Asn⁴⁸⁷. Flexibility of this segment is proposed to induce the "open" state of the pocket and accommodate the bulky probe inside so that the consequential irreversible shifts in the pocket constituents disassemble GroEL. This scheme is supported by the finding that DTP-induced disassembly of GroEL is facilitated by ATP, which specifically stimulates a local shift of the segment Asn⁴⁷⁵-Asn⁴⁸⁷ into solution.

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Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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