The unfolding story of the Escherichia coli Hsp70 DnaK: Is DnaK a holdase or an unfoldase?

Molecular Microbiology

Volumn 45, Issue 5, 2002, Pages 1197-1206

  Slepenkov, Sergey V ^a   Witt, Stephan N ^a  

^a LOUISIANA STATE UNIVERSITY HEALTH SCIENCES CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; CHAPERONE; HEAT SHOCK PROTEIN 70; LIGAND; PROTEIN DNAK;

ESCHERICHIA COLI; HYDROLYSIS; MOLECULAR DYNAMICS; MOLECULAR MECHANICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PROCESSING; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; SHORT SURVEY; SIMULATION; TRANSLATION REGULATION;

ADENOSINE TRIPHOSPHATE; COMPUTER SIMULATION; ESCHERICHIA COLI PROTEINS; HSP70 HEAT-SHOCK PROTEINS; MODELS, BIOLOGICAL; MODELS, MOLECULAR; MOLECULAR CHAPERONES; PROTEIN BIOSYNTHESIS; PROTEIN FOLDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, TERTIARY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0036049850     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2002.03093.x     Document Type: Short Survey

References (44)

1. Roles of molecular chaperones in cytoplasmic protein folding
2. Principles that govern the folding of protein chains
3. Analysis of numerical methods for computer simulation of kinetic processes: Development of KINSIM - A flexible, portable system
4. The Hsp70 and Hsp60 chaperone machines
5. Trigger factor and DnaK cooperate in folding of newly synthesized proteins
6. Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery
7. Principles of protein folding in the cellular environment
8. Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein
9. Catapult mechanism renders the chaperone action of Hsp70 unidirectional
10. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
11. Specificity of DnaK-peptide binding
12. Kinetics of nucleotide-induced changes in the tryptophan fluorescence of the molecular chaperone Hsc70 and its subfragments suggest the ATP-induced conformational change follows initial ATP binding
13. Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK
14. The role of heat-shock and chaperone proteins in protein folding: Possible molecular mechanisms
15. Modulation of the ATPase activity of the molecular chaperone DnaK by peptides and the DnaJ and GrpE heat shock proteins
16. A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein
17. The J-domain family and the recruitment of chaperone power
18. Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones
19. GrpE accelerates peptide binding and release from the high-affinity state of DnaK
20. Investigation of the interaction between DnaK and DnaJ by surface plasmon resonance spectroscopy
21. A GrpE mutant containing the NH(2)-terminal 'tail' region is able to displace bound polypeptide substrate from DnaK
22. J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences
23. Identification of thermolabile Escherichia coli proteins: Prevention and reversion of aggregation by DnaK and ClpB
24. The peptide-binding domain of the chaperone protein HSC 70 has an unusual secondary structure topology
25. GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism
26. ATP-induced protein-Hsp70 complex dissociation requires K+ but not ATP hydrolysis
27. The power stroke of the DnaK/DnaJ/GrpE molecular chaperone system
28. Sequence-specific rates of interaction of target peptides with the molecular chaperone DnaK and DnaJ
29. Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cells
30. Cell biology. An unfolding story of protein translocation
31. Its substrate specificity characterizes the DnaJ cochaperone as a scanning factor for the DnaK chaperone
32. Kinetic characterization of the ATPase cycle of the DnaK molecular chaperone
33. DnaJ dramatically stimulates ATP hydrolysis by DnaK: Insight into targeting of Hsp70 proteins to polypeptide substrates
34. Kinetics of molecular chaperone action
35. Chaperonin function: Folding by forced unfolding
36. Peptide-induced conformational changes in the molecular chaperone DnaK
37. Structural features required for the interaction of the Hsp70 molecular chaperone DnaK with its cochaperone DnaJ
38. Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains
39. The second step of ATP binding to DnaK induces peptide release
40. The protein import motor of mitochondria: Unfolding and trapping of preproteins are distinct and separable functions of matrix Hsp70
41. Unraveling the kinetic mechanism of the 70-kDa molecular chaperones using fluorescence spectroscopic methods
42. Structural analysis of substrate binding by the molecular chaperone DnaK
43. Estimation of macromolecule concentrations and excluded Volume effects for the cytoplasm ofEscherichia coli