Category:Complex:DnaJ/DnaK/GrpE

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Description (originally from EcoCyc[1][2]) DnaJ/DnaK/GrpE

Comments (originally from EcoCyc[1][2]) The DnaK system of E. coli is a homolog of the eukaryotic Hsp70 chaperone system. This chaperone system assists in a number of cytoplasmic cellular processes including folding of nascent polypeptide chains, rescue of misfolded proteins, polypeptide chain translocation through membranes, assembly and disassembly of protein complexes, and control of folded regulatory proteins' biological activity. The chaperone action of DnaK is powered by ATP hydrolysis and is assisted by partner chaperones DnaJ and GrpE [3][4][3][5][6][7][8][9][10].


References

  1. ↑ 1.0 1.1 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  2. ↑ 2.0 2.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ 3.0 3.1 Bukau, B & Horwich, AL (1998) The Hsp70 and Hsp60 chaperone machines. Cell 92 351-66 PubMed
  4. ↑ Zhu, X et al. (1996) Structural analysis of substrate binding by the molecular chaperone DnaK. Science 272 1606-14 PubMed
  5. ↑ Ha, JH & McKay, DB (1995) 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. Biochemistry 34 11635-44 PubMed
  6. ↑ Wall, D et al. (1994) The NH2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for lambda replication. J. Biol. Chem. 269 5446-51 PubMed
  7. ↑ Liberek, K et al. (1991) Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc. Natl. Acad. Sci. U.S.A. 88 2874-8 PubMed
  8. ↑ Grimshaw, JP et al. (2003) Thermosensor action of GrpE. The DnaK chaperone system at heat shock temperatures. J. Biol. Chem. 278 19048-53 PubMed
  9. ↑ Fredriksson, A et al. (2005) Defense against protein carbonylation by DnaK/DnaJ and proteases of the heat shock regulon. J. Bacteriol. 187 4207-13 PubMed
  10. ↑ Mogk, A et al. (2003) Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation. Mol. Microbiol. 50 585-95 PubMed

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