Journal: J Biol Chem / Year: 2013 Title: Structural insights into the chaperone activity of the 40-kDa heat shock protein DnaJ: binding and remodeling of a native substrate. Authors: Jorge Cuéllar / Judit Perales-Calvo / Arturo Muga / José María Valpuesta / Fernando Moro / Abstract: Hsp40 chaperones bind and transfer substrate proteins to Hsp70s and regulate their ATPase activity. The interaction of Hsp40s with native proteins modifies their structure and function. A good model ...Hsp40 chaperones bind and transfer substrate proteins to Hsp70s and regulate their ATPase activity. The interaction of Hsp40s with native proteins modifies their structure and function. A good model for this function is DnaJ, the bacterial Hsp40 that interacts with RepE, the repressor/activator of plasmid F replication, and together with DnaK regulates its function. We characterize here the structure of the DnaJ-RepE complex by electron microscopy, the first described structure of a complex between an Hsp40 and a client protein. The comparison of the complexes of DnaJ with two RepE mutants reveals an intrinsic plasticity of the DnaJ dimer that allows the chaperone to adapt to different substrates. We also show that DnaJ induces conformational changes in dimeric RepE, which increase the intermonomeric distance and remodel both RepE domains enhancing its affinity for DNA.
History
Deposition
Mar 15, 2013
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Header (metadata) release
Apr 17, 2013
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Map release
Apr 24, 2013
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Update
Dec 25, 2013
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Current status
Dec 25, 2013
Processing site: PDBe / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
Type: NEGATIVE Details: Samples (either DnaJ:RepE, DnaJ:RepE1-144 or DnaJ:RepE54 complexes) were diluted 1:100 in 20mM Hepes pH 7.4, 50mM KCl, 5mM DTT and 0.1mM EDTA buffer, applied onto carbon-coated copper grids ...Details: Samples (either DnaJ:RepE, DnaJ:RepE1-144 or DnaJ:RepE54 complexes) were diluted 1:100 in 20mM Hepes pH 7.4, 50mM KCl, 5mM DTT and 0.1mM EDTA buffer, applied onto carbon-coated copper grids and stained with 2% uranyl acetate.
Grid
Details: 300 mesh Cu/Rh grid with thin carbon support and glow discharged
Vitrification
Cryogen name: NONE / Instrument: OTHER
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Electron microscopy
Microscope
JEOL 1200EXII
Alignment procedure
Legacy - Astigmatism: Objective lens astigmatism was corrected at 100,000 times magnification
Details
Additional details about microscope model:JEOL 1200EXII
Date
Oct 5, 2009
Image recording
Category: FILM / Film or detector model: KODAK SO-163 FILM / Digitization - Scanner: ZEISS SCAI / Digitization - Sampling interval: 14 µm / Number real images: 320 / Average electron dose: 10 e/Å2 / Bits/pixel: 8
Electron beam
Acceleration voltage: 100 kV / Electron source: TUNGSTEN HAIRPIN
Electron optics
Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 5.6 mm / Nominal magnification: 60000
Sample stage
Specimen holder model: JEOL
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Image processing
Details
The particles were selected by manual picking
CTF correction
Details: CTFFIND
Final reconstruction
Applied symmetry - Point group: C1 (asymmetric) / Algorithm: OTHER / Resolution.type: BY AUTHOR / Resolution: 19.0 Å / Resolution method: FSC 0.5 CUT-OFF / Software - Name: EMAN, XMIPP / Number images used: 14327
Final two d classification
Number classes: 75
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