The unfolding action of GroEL on a protein substrate

Biophysical Journal
Arjan van der VaartM Karplus

Abstract

A molecular dynamics simulation of the active unfolding of denatured rhodanese by the chaperone GroEL is presented. The compact denatured protein is bound initially to the cis cavity and forms stable contacts with several of the subunits. As the cis ring apical domains of GroEL undergo the transition from the closed to the more open (ATP-bound) state, they exert a force on rhodanese that leads to the increased unfolding of certain loops. The contacts between GroEL and rhodanese are analyzed and their variation during the GroEL transition is shown. The major contacts, which give rise to the stretching force, are found to be similar to those observed in crystal structures of peptides bound to the apical domains. The results of the simulation show that multidomain interactions play an essential role, in accord with experiments. Implications of the results for mutation experiments and for the action of GroEL are discussed.

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Citations

Feb 23, 2013·Cell Stress & Chaperones·Andrija Finka, Pierre Goloubinoff
Jun 22, 2005·Journal of Molecular Biology·George StanD Thirumalai
May 15, 2007·Proceedings of the National Academy of Sciences of the United States of America·George StanBernard R Brooks
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May 13, 2006·Annual Review of Biophysics and Biomolecular Structure·Martin Karplus
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Apr 20, 2005·The Journal of Chemical Physics·Arjan van der Vaart, Martin Karplus
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