dnaK Antibody

1. While preventing the formation of lethal IpaC aggregates, DnaK promoted the incorporation of IpaC into large and dynamic complexes (LDCs) restricted at the bacterial pole through nucleoid occlusion. Direct and reversible IpaC-DnaK interactions as part of large dynamic complexes (LDCs) drive polarization through nucleoid occlusion. Polar accumulation was associated with DnaKJ-dependent substrate folding. PMID: 29795186
2. BAH1, an E3 ligase from plant that has a similar zinc finger domain to DnaJ, can perform block the effect of DnaK on sigma(32) in Escherichia coli. PMID: 29260303
3. A folding nucleus and minimal ATP binding domain of Hsp70 identified by single-molecule force spectroscopy. PMID: 29669923
4. the mutant K-12 DeltadnaK was more sensitive to Ultrasound with c. 2.5 log (CFU per ml) reduction in comparison to their isogenic wild-type E. coli K-12. This indicates that the dnaK gene participates in general stress response and more specifically to hyperosmotic stress. PMID: 28727911
5. The results provide new insight into the heterogeneous ensemble of complexes formed by DnaK chaperones. PMID: 28833766
6. Taken together, these results suggest that a specific region in the nucleotide-binding domain of DnaK is involved in the interaction with Escherichia coli Hsp90, and this interaction is functionally important. PMID: 28013030
7. binding of a peptide substrate to the DnaK-peptide-binding domain leads to prominent lid closure. PMID: 27248857
8. the helical lid of DnaK is a highly dynamic unit of the structure in all ligand-bound states. Importantly, we demonstrate that DnaK populates a partially docked state in the presence of ATP and substrate and that this state represents an energy minimum on the DnaK allosteric landscape. PMID: 28428246
9. this study shows that DnaK has the potential to modify and enhance immunogenicity when associated with aggregated protein PMID: 27859059
10. Fatty acid methyl esters analysis indicated that the amount of unsaturated fatty acid sharply increased and subcellular location prediction analysis showed a marked decrease in transcription of inner-membrane protein genes, which might have triggered the development of aberrant cell shape and susceptibility for some antibiotics in the DeltadnaKJ strain. PMID: 27242140
11. we observe an additive effect of DnaK and GroEL chaperones on the evolutionary rates of their common interactors. Finally, we found pronounced similarities in the physicochemical profiles that characterize proteins belonging to DnaK and GroEL interactomes. PMID: 27189986
12. For DnaK, acetyl-CoA carboxylase, biotin carboxylase subunit (AccC) and phosphate acetyltransferase (Pta) we also showed a direct role of PpiB in the functional control of these proteins because it increased the measured enzyme activity of each protein and further interfered with DnaK localization and the correct folding of AccC. PMID: 27306110
13. Data show that a partially docked DnaK structure is achieved by combining ATP in the the N-terminal nucleotide binding domain (NBD) and peptide in the substrate binding domain (SBD). PMID: 27025773
14. This unit describes the procedure for following reactivation of an aggregated enzyme glucose-6-phosphate dehydrogenase mediated by ClpB from Escherichia coli in cooperation with another molecular chaperone, DnaK. PMID: 26836408
15. The interaction of DnaK with DnaJ, GrpE, or sigma32 becomes weaker when DnaK is glutathionylated during oxidative stress, and the interaction is restored upon deglutathionylation. PMID: 26823468
16. Data suggest that neither DnaK nor GroEL singly can modulate sigma32 stability in vivo; there is ordered network between them, where GroEL acts upstream of DnaK. PMID: 26545493
17. analysis of human telomere repeat binding factor 1 (hTRF1) in complex with Escherichia coli Hsp70 (DnaK) PMID: 26240333
18. the C-terminal helix of the nucleotide binding domain of the Hsp70 chaperone DnaK is the major determinant of mechanical stability PMID: 26240360
19. analysis of DnaJ-DnaK-GrpE chaperone cooperation PMID: 25686738
20. The nucleotide exchange factor GrpE modulates the chaperone DnaK allosterism. PMID: 25739641
21. Dnak and substrate proteins regulate the ATPase activity and dynamics of ClpB. PMID: 25558912
22. E. coli DnaK variants with substitutions in subdomains IB and IIB of the nucleotide-binding domain are defective for in vivo and in vitro interactions with ClpB. PMID: 25451597
23. Used molecular dynamics simulations, mutagenesis, and enzymatic assays to explore the molecular basis of the structure and function of E coli DnaK. PMID: 24277995
24. DnaJ-promoted binding of DnaK to multiple sites on sigma32 in the presence of ATP. PMID: 24532774
25. Data indicate that ClpB requires DnaK more stringently than Hsp104 requires Hsp70 for protein disaggregation. PMID: 24280225
26. The ATP-bound nucleotide-binding domain of DnaK forms extensive interfaces with a substrate-binding domain that has changed its alpha-helical lid displaced PMID: 23708608
27. The DnaK chaperone has evolved to bind peptides in both orientations in the substrate binding cleft with comparable energy without rearrangements of the protein. PMID: 23562829
28. Trigger factor dependent refolding of bacterial luciferases in Escherichia coli cells: kinetics, efficiency and effect of the bichaperone system, DnaKJE-ClpB PMID: 23888781
29. Disruption of the TF/DnaK chaperone pathway is rescued by overexpression of the redox-regulated chaperone Hsp33. PMID: 23148222
30. The "allosterically active" state for the E. coli Hsp70, DnaK, trapped and identified how interactions among the nucleotide-binding domain (NBD), the beta subdomain of the substrate-binding domain (SBD), the SBD alpha-helical lid, and the conserved hydrophobic interdomain linker enable allosteric signal transmission between ligand-binding sites. PMID: 23217711
31. The analysis revealed that nearly every protein is predicted to contain multiple DnaK- and DnaJ-binding sites, with the DnaJ sites occurring approximately twice as often. PMID: 22732719
32. DnaK oligomers are composed of ordered multimers that are functionally distinct from monomeric DnaK. PMID: 22076723
33. The authors demonstrate that DksA expression from a multicopy plasmid is necessary and sufficient for suppression of dnaKJ deletion mutation. PMID: 22267514
34. mutation of specific conserved sites within the DnaK C terminus reduces the capacity of the cell to withstand stresses on protein folding caused by elevated temperature or the absence of other chaperones PMID: 21768118
35. Results indicate that E. coli Hsp90 and DnaK interact in vivo and in vitro, providing additional evidence to suggest that E. coli Hsp90 and the DnaK system function together PMID: 21525416
36. Ribosome assembly defects at very high temperature are partially compensated by plasmid-driven overexpression of the DnaK chaperone. PMID: 21059683
37. analysis of complex relationships between ATPase rate and the chaperone activities of Escherichia coli heat shock protein 70 (Hsp70/DnaK) PMID: 20439464
38. the Hsp40 J-domain (Jd) shifts DnaK to a client-bound form by stimulating the DnaK ATPase but only when the Jd is brought to DnaK by a client-Hsp40 complex PMID: 20448033
39. the interaction of DnaK and its co-chaperones with aggregated substrate is the rate-limiting reaction at the initial steps of disaggregation PMID: 15302880
40. results indicate that, despite their high structural identity (approximately 80%) and similar mechanisms of action, the DnaK chaperones of closely related V. harveyi and E.coli bacteria differ functionally. PMID: 15448982
41. DnaK-DnaJ-GrpE chaperone system has a role in activating the pi initiator protein PMID: 15485812
42. data demonstrates CD154-independent CD40 activation in polymicrobial sepsis and suggests that bacterial HSP70 is capable of stimulating CD40 in vitro and in vivo PMID: 15545825
43. Data describe the trigger factor concentration dependence of the glyceraldehyde-3-phosphate dehydrogenase reactivation yield in the presence and absence of the DnaK-DnaJ-GrpE chaperone system in vitro. PMID: 15632130
44. Upon oxidative stress, DnaK's N terminus reversibly unfolds in vivo, and DnaK loses its ability to protect proteins against stress-induced aggregation. PMID: 15694339
45. DnaK and DnaJ molecular chaperones apparently influence the amount of tryptophanase, the expression of which is regulated at all transcription steps, including transcription elongation. PMID: 15702537
46. direct thermal adaptation of the DnaK chaperone system by thermosensing GrpE is essential for efficient chaperone action during heat shock PMID: 15705578
47. Results indicate that the complex between DnaK384-638 and its substrate forms a rigid conformation in the beta-domain. PMID: 15752686
48. ATPase activity of DnaK is not connected to structural changes of the peptide-binding pocket but rather only has an effect on the LID domain or other further remote residues PMID: 15784262
49. chaperones DnaK and GroEL have been identified at the solvent-exposed surface of bacterial inclusion bodies and entrapped within these aggregates, respectively PMID: 15866952
50. Separate overproduction of the major chaperone systems, DnaK/DnaJ and GroEL/GroES, established that the former of these is more important in counteracting protein carbonylation. PMID: 15937182

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KEGG: ecj:JW0013

STRING: 316385.ECDH10B_0014