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

AutorMelero, Roberto ; Moro, Fernando; Pérez-Calvo, María Ángeles; Perales-Calvo, Judit; Quintana-Gallardo, Lucía; Llorca, Óscar ; Muga, Arturo; Valpuesta, José María
Palabras clave70-Kilodalton heat shock protein (Hsp70)
Chaperone
Chaperone DnaK (DnaK)
Electron microscopy (EM)
GrpE
Nucleotide exchange factor
Protein folding
Fecha de publicación4-mar-2015
EditorAmerican Society for Biochemistry and Molecular Biology
CitaciónJ Biol Chem.290(16):10083-92 (2015)
ResumenHsp70 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.
Descripción10 p.-6 fig.
Versión del editorhttp://dx.doi.org/10.1074/jbc.M114.623371
URIhttp://hdl.handle.net/10261/154158
DOI10.1074/jbc.M114.623371
ISSN0021-9258
E-ISSN1083-351X
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