Structural highlights
Function
DNAJ_ECOLI Interacts with DnaK and GrpE to disassemble a protein complex at the origins of replication of phage lambda and several plasmids. Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.[1] [2] [3] [4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
See Also
References
- ↑ Liberek K, Marszalek J, Ang D, Georgopoulos C, Zylicz M. Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc Natl Acad Sci U S A. 1991 Apr 1;88(7):2874-8. PMID:1826368
- ↑ Zietkiewicz S, Krzewska J, Liberek K. Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation. J Biol Chem. 2004 Oct 22;279(43):44376-83. Epub 2004 Aug 9. PMID:15302880 doi:http://dx.doi.org/10.1074/jbc.M402405200
- ↑ Siegenthaler RK, Grimshaw JP, Christen P. Immediate response of the DnaK molecular chaperone system to heat shock. FEBS Lett. 2004 Mar 26;562(1-3):105-10. PMID:15044009 doi:http://dx.doi.org/10.1016/S0014-5793(04)00190-5
- ↑ Zzaman S, Reddy JM, Bastia D. The DnaK-DnaJ-GrpE chaperone system activates inert wild type pi initiator protein of R6K into a form active in replication initiation. J Biol Chem. 2004 Dec 3;279(49):50886-94. Epub 2004 Oct 13. PMID:15485812 doi:http://dx.doi.org/M407531200
