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A more recent version of this article appeared on October 29, 2004
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M406795200v1
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Papers In Press, published online ahead of print August 30, 2004
J. Biol. Chem, 10.1074/jbc.M406795200
Submitted on June 17, 2004
Revised on August 26, 2004
Accepted on August 30, 2004

BeFx stops 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

Chemical Resources Laboratory, Tokyo Institute of Technology, Yokohama, Yokohama 226-8503

Corresponding Author: myoshida{at}res.titech.ac.jp

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


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