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Differential conformational modulations of MreB folding upon interactions with GroEL/ES and TRiC chaperonin components

Authors :
Renaud Vincentelli
Jérôme Wenger
Uno Carlsson
Bengt-Harald Jonsson
Satish Babu Moparthi
Per Hammarström
MOSAIC (MOSAIC)
Institut FRESNEL (FRESNEL)
Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)-Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)-Centre National de la Recherche Scientifique (CNRS)
Department of Physics, Chemistry and Biology [Linköping] (IFM)
Linköping University (LIU)
Architecture et fonction des macromolécules biologiques (AFMB)
Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)
European Project: 278242,EC:FP7:ERC,ERC-2011-StG_20101014,EXTENDFRET(2012)
Centre National de la Recherche Scientifique (CNRS)-École Centrale de Marseille (ECM)-Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)-École Centrale de Marseille (ECM)-Aix Marseille Université (AMU)
Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA)
Source :
Scientific Reports, Scientific Reports, Nature Publishing Group, 2016, 6, pp.28386. ⟨10.1038/srep28386⟩, Scientific Reports, 2016, 6, pp.28386. ⟨10.1038/srep28386⟩
Publication Year :
2016
Publisher :
HAL CCSD, 2016.

Abstract

Here, we study and compare the mechanisms of action of the GroEL/GroES and the TRiC chaperonin systems on MreB client protein variants extracted from E. coli. MreB is a homologue to actin in prokaryotes. Single-molecule fluorescence correlation spectroscopy (FCS) and time-resolved fluorescence polarization anisotropy report the binding interaction of folding MreB with GroEL, GroES and TRiC. Fluorescence resonance energy transfer (FRET) measurements on MreB variants quantified molecular distance changes occurring during conformational rearrangements within folding MreB bound to chaperonins. We observed that the MreB structure is rearranged by a binding-induced expansion mechanism in TRiC, GroEL and GroES. These results are quantitatively comparable to the structural rearrangements found during the interaction of beta-actin with GroEL and TRiC, indicating that the mechanism of chaperonins is conserved during evolution. The chaperonin-bound MreB is also significantly compacted after addition of AMP-PNP for both the GroEL/ES and TRiC systems. Most importantly, our results showed that GroES may act as an unfoldase by inducing a dramatic initial expansion of MreB (even more than for GroEL) implicating a role for MreB folding, allowing us to suggest a delivery mechanism for GroES to GroEL in prokaryotes. Funding Agencies|European Commission [FP7-ICT-2011-7, ERC StG 278242]; Goran Gustafsson Foundation; Swedish Alzheimer Foundation

Details

Language :
English
ISSN :
20452322
Database :
OpenAIRE
Journal :
Scientific Reports, Scientific Reports, Nature Publishing Group, 2016, 6, pp.28386. ⟨10.1038/srep28386⟩, Scientific Reports, 2016, 6, pp.28386. ⟨10.1038/srep28386⟩
Accession number :
edsair.doi.dedup.....4d2082067122990cd6032cc302d88c6d
Full Text :
https://doi.org/10.1038/srep28386⟩