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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Llorca, Oscar Moro, Fernando Pérez-calvo, María Ángeles Quintana-gallardo, Lucía Muga, Arturo Melero, Roberto Perales-calvo, Judit Valpuesta, José María |
| Description | Author Affiliation: Melero R ( From the Centro de Investigaciones Biológicas (CIB-CSIC), 28040 Madrid.); Moro F ( the Unidad de Biofísica (CSIC/UPV-EHU) and Departamento de Bioquímica y Biología Molecular, Facultad de Ciencia y Tecnología, Universidad del País Vasco, 48080 Bilbao, and.); Pérez-Calvo MÁ ( the Centro Nacional de Biotecnología (CNB-CSIC), 28049 Madrid, Spain.); Perales-Calvo J ( the Unidad de Biofísica (CSIC/UPV-EHU) and Departamento de Bioquímica y Biología Molecular, Facultad de Ciencia y Tecnología, Universidad del País Vasco, 48080 Bilbao, and.); Quintana-Gallardo L ( the Centro Nacional de Biotecnología (CNB-CSIC), 28049 Madrid, Spain.); Llorca O ( From the Centro de Investigaciones Biológicas (CIB-CSIC), 28040 Madrid, ollorca@cib.csic.es.); Muga A ( the Unidad de Biofísica (CSIC/UPV-EHU) and Departamento de Bioquímica y Biología Molecular, Facultad de Ciencia y Tecnología, Universidad del País Vasco, 48080 Bilbao, and arturo.muga@ehu.es.); Valpuesta JM ( the Centro Nacional de Biotecnología (CNB-CSIC), 28049 Madrid, Spain jmv@cnb.csic.es.) |
| Abstract | Hsp70 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. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 16 |
| Volume Number | 290 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2015-04-17 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Adenosine Diphosphate Chemistry Adenosine Triphosphate Escherichia Coli Proteins Escherichia Coli HSP70 Heat-Shock Proteins Heat-Shock Proteins Metabolism Allosteric Regulation Crystallography, X-Ray Genetics Gene Expression Models, Molecular Protein Binding Protein Multimerization Protein Structure, Secondary Protein Structure, Tertiary Recombinant Proteins Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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