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

The Biochemical Journal
Tomoya SameshimaT Funatsu

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.

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Citations

Jun 1, 2010·The Journal of Biological Chemistry·Tomoya SameshimaTakashi Funatsu
Apr 21, 2012·The Journal of Biological Chemistry·Yi-Chin C TsaiManajit Hayer-Hartl
Oct 11, 2012·The Journal of Biological Chemistry·Yodai TakeiTakashi Funatsu
Oct 30, 2013·Proceedings of the National Academy of Sciences of the United States of America·Xiang Ye, George H Lorimer
Oct 30, 2013·Proceedings of the National Academy of Sciences of the United States of America·Dong YangGeorge H Lorimer
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