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J. Biol. Chem., Vol. 279, Issue 44, 45737-45743, October 29, 2004

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BeF_x Stops the Chaperonin Cycle of GroEL-GroES and Generates a Complex with Double Folding Chambers^*

Hideki Taguchi¶, Keigo Tsukuda, Fumihiro Motojima, Ayumi Koike-Takeshita, and Masasuke Yoshida||

From the Chemical Resources Laboratory, Tokyo Institute of Technology, 4259 Nagatsuta, Yokohama, 226-8503, Japan, Precursory Research for Embryonic Science and Technology (PRESTO), Japan Science and Technology Agency, 4-1-8 Honcho Kawaguchi, Saitama, 332-0012, Japan

Coupling with ATP hydrolysis and cooperating with GroES, the double ring chaperonin GroEL assists the folding of other proteins. Here we report novel GroEL-GroES complexes formed in fluoroberyllate (BeF_x) that can mimic the phosphate part of the enzyme-bound nucleotides. In ATP, BeF_x stops the functional turnover of GroEL by preventing GroES release and produces a symmetric 1:2 GroEL-GroES complex in which both GroEL rings contain ADP·BeF_x and an encapsulated substrate protein. In ADP, the substrate protein-loaded GroEL cannot bind GroES. In ADP plus BeF_x, however, it can bind GroES to form a stable 1:1 GroEL-GroES complex in which one of GroEL rings contains ADP·BeF_x and an encapsulated substrate protein. This 1:1 GroEL-GroES complex is converted into the symmetric 1:2 GroEL-GroES complex when GroES is supplied in ATP plus BeF_x. Thus, BeF_x stabilizes two GroEL-GroES complexes; one with a single folding chamber and the other with double folding chambers. These results shed light on the intermediate ADP·P_i nucleotide states in the functional cycle of GroEL.

Received for publication, June 17, 2004 , and in revised form, August 26, 2004.

^* This work was supported in part by grants-in-aid for Scientific Research on Priority Areas (to H. T. and M. Y.) from the Ministry of Education, Culture, Sports, Science, and Technology of Japan. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ Present address: Dept. of Medical Genome Sciences, Graduate School of Frontier Sciences, The University of Tokyo, Kashiwa, Chiba 277-8562, Japan.

^|| To whom correspondence should be addressed: Chemical Resources Laboratory, R1-7, Tokyo Institute of Technology, 4259 Nagatsuta, Yokohama, 226-8503, Japan. Tel.: 81-45-924-5233; Fax: 81-45-924-5277; E-mail: myoshida{at}res.titech.ac.jp.

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