Structural basis of substrate progression through the bacterial chaperonin cycle

Author:

Gardner Scott1ORCID,Darrow Michele C.2,Lukoyanova Natalya1ORCID,Thalassinos Konstantinos13ORCID,Saibil Helen R.1ORCID

Affiliation:

1. Institute of Structural and Molecular Biology, Department of Biological Sciences, Birkbeck, University of London, London WC1E 7HX, United Kingdom

2. SPT Labtech, Melbourn, Cambridge SG8 6HB, United Kingdom

3. Division of Biosciences, Institute of Structural and Molecular Biology, University College London, London WC1E 6BT, United Kingdom

Abstract

The bacterial chaperonin GroEL-GroES promotes protein folding through ATP-regulated cycles of substrate protein binding, encapsulation, and release. Here, we have used cryoEM to determine structures of GroEL, GroEL-ADP·BeF 3 , and GroEL-ADP·AlF 3 -GroES all complexed with the model substrate Rubisco. Our structures provide a series of snapshots that show how the conformation and interactions of non-native Rubisco change as it proceeds through the GroEL-GroES reaction cycle. We observe specific charged and hydrophobic GroEL residues forming strong initial contacts with non-native Rubisco. Binding of ATP or ADP·BeF 3 to GroEL-Rubisco results in the formation of an intermediate GroEL complex displaying striking asymmetry in the ATP/ADP·BeF 3 -bound ring. In this ring, four GroEL subunits bind Rubisco and the other three are in the GroES-accepting conformation, suggesting how GroEL can recruit GroES without releasing bound substrate. Our cryoEM structures of stalled GroEL-ADP·AlF 3 -Rubisco-GroES complexes show Rubisco folding intermediates interacting with GroEL-GroES via different sets of residues.

Funder

UKRI | Biotechnology and Biological Sciences Research Council

Wellcome Trust

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

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