English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/154158
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE
Exportar a otros formatos:

Title

Modulation of the chaperone DnaK allosterism by the nucleotide exchange factor GrpE

AuthorsMelero, Roberto ; Moro, Fernando; Pérez-Calvo, María Ángeles; Perales-Calvo, Judit; Quintana-Gallardo, Lucía; Llorca, Óscar ; Muga, Arturo; Valpuesta, José M.
Keywords70-Kilodalton heat shock protein (Hsp70)
Chaperone
Chaperone DnaK (DnaK)
Electron microscopy (EM)
GrpE
Nucleotide exchange factor
Protein folding
Issue Date4-Mar-2015
PublisherAmerican Society for Biochemistry and Molecular Biology
CitationJ Biol Chem.290(16):10083-92 (2015)
AbstractHsp70 chaperones comprise two domains, the nucleotide-binding domain (Hsp70NBD), responsible for structural and functional changes in the chaperone, and the substrate-binding domain (Hsp70SBD), involved in substrate interaction. Substrate binding and release in Hsp70 is controlled by the nucleotide state of DnaKNBD, with ATP inducing the open, substrate-receptive DnaKSBD conformation, whereas ADP forces its closure. DnaK cycles between the two conformations through interaction with two cofactors, the Hsp40 co-chaperones (DnaJ in Escherichia coli) induce the ADP state, and the nucleotide exchange factors (GrpE in E. coli) induce the ATP state. X-ray crystallography showed that the GrpE dimer is a nucleotide exchange factor that works by interaction of one of its monomers with DnaKNBD. DnaKSBD location in this complex is debated; there is evidence that it interacts with the GrpE N-terminal disordered region, far from DnaKNBD. Although we confirmed this interaction using biochemical and biophysical techniques, our EM-based three-dimensional reconstruction of the DnaK-GrpE complex located DnaKSBD near DnaKNBD. This apparent discrepancy between the functional and structural results is explained by our finding that the tail region of the GrpE dimer in the DnaK-GrpE complex bends and its tip contacts DnaKSBD, whereas the DnaKNBD-DnaKSBD linker contacts the GrpE helical region. We suggest that these interactions define a more complex role for GrpE in the control of DnaK function.
Description10 p.-6 fig.
Publisher version (URL)http://dx.doi.org/10.1074/jbc.M114.623371
URIhttp://hdl.handle.net/10261/154158
DOIhttp://dx.doi.org/10.1074/jbc.M114.623371
ISSN0021-9258
E-ISSN1083-351X
Appears in Collections:(CIB) Artículos
Files in This Item:
File Description SizeFormat 
JBC 2015.pdfArtículo principal1,66 MBAdobe PDFThumbnail
View/Open
Show full item record
Review this work
 


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.