Structural Features Required for the Interaction of the Hsp70 Molecular Chaperone DnaK with Its Cochaperone DnaJ
Open Access
- 1 October 1999
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 274 (43), 30534-30539
- https://doi.org/10.1074/jbc.274.43.30534
Abstract
No abstract availableKeywords
This publication has 30 references indexed in Scilit:
- Peptide-Induced Conformational Changes in the Molecular Chaperone DnaKBiochemistry, 1998
- The power stroke of the DnaK/DnaJ/GrpE molecular chaperone system 1 1Edited by J.KarnJournal of Molecular Biology, 1997
- Interaction of Hsp70 chaperones with substratesNature Structural & Molecular Biology, 1997
- A function for the QKRAA amino acid motif: mediating binding of DnaJ to DnaK. Implications for the association of rheumatoid arthritis with HLA-DR4.Journal of Clinical Investigation, 1997
- A Bipartite Signaling Mechanism Involved in DnaJ-mediated Activation of the Escherichia coli DnaK ProteinJournal of Biological Chemistry, 1996
- Conformational Characterization of DnaK and Its Complexes by Small-Angle X-ray ScatteringBiochemistry, 1996
- Analysis of Three DnaK Mutant Proteins Suggests That Progression through the ATPase Cycle Requires Conformational ChangesPublished by Elsevier ,1995
- Divergent Effects of ATP on the Binding of the DnaK and DnaJ Chaperones to Each Other, or to Their Various Native and Denatured Protein SubstratesJournal of Biological Chemistry, 1995
- ATP-induced protein Hsp70 complex dissociation requires K+ but not ATP hydrolysisNature, 1993
- Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate proteinNature, 1990