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Differential conformational modulations of MreB folding upon interactions with GroEL/ES and TRiC chaperonin components
- 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
- Subjects :
- 0301 basic medicine
Models, Molecular
Protein Folding
Protein Conformation
Biophysics
macromolecular substances
Biology
MreB
Article
Chaperonin
03 medical and health sciences
Protein structure
Chaperonin 10
Escherichia coli
Fluorescence Resonance Energy Transfer
[SPI.NANO]Engineering Sciences [physics]/Micro and nanotechnologies/Microelectronics
Actin
MreB protein
[PHYS.PHYS.PHYS-OPTICS]Physics [physics]/Physics [physics]/Optics [physics.optics]
Multidisciplinary
030102 biochemistry & molecular biology
Escherichia coli Proteins
Fluorescence Resonance Energy Transfer FRET
GroES
Chaperonin 60
GroEL
Biofysik
Actins
Single Molecule Imaging
Cell biology
Protein Structure, Tertiary
enzymes and coenzymes (carbohydrates)
030104 developmental biology
Förster resonance energy transfer
Mutation
biological sciences
[SPI.OPTI]Engineering Sciences [physics]/Optics / Photonic
bacteria
Protein folding
sense organs
Chaperonin Containing TCP-1
Protein Binding
Subjects
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⟩