Denatured proteins facilitate the formation of the football-shaped GroEL–(GroES)2 complex

Author:

Sameshima Tomoya1,Iizuka Ryo1,Ueno Taro12,Funatsu Takashi134

Affiliation:

1. Laboratory of Bio-analytical Chemistry, Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan

2. Department of Chemistry, Stanford University, Stanford, CA 94305-5080, U.S.A.

3. Center for NanoBio Integration, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan

4. Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Corporation (JST), 5 Sanbancho, Chiyoda-ku, Tokyo 102-0075, Japan

Abstract

Controversy exists over whether the chaperonin GroEL forms a GroEL–(GroES)2 complex (football-shaped complex) during its reaction cycle. We have revealed previously the existence of the football-shaped complex in the chaperonin reaction cycle using a FRET (fluorescence resonance energy transfer) assay [Sameshima, Ueno, Iizuka, Ishii, Terada, Okabe and Funatsu (2008) J. Biol. Chem. 283, 23765–23773]. Although denatured proteins alter the ATPase activity of GroEL and the dynamics of the GroEL–GroES interaction, the effect of denatured proteins on the formation of the football-shaped complex has not been characterized. In the present study, a FRET assay was used to demonstrate that denatured proteins facilitate the formation of the football-shaped complex. The presence of denatured proteins was also found to increase the rate of association of GroES to the trans-ring of GroEL. Furthermore, denatured proteins decrease the inhibitory influence of ADP on ATP-induced association of GroES to the trans-ring of GroEL. From these findings we conclude that denatured proteins facilitate the dissociation of ADP from the trans-ring of GroEL and the concomitant association of ATP and the second GroES.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference42 articles.

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