Category:Complex:ClpX ATP-dependent protease specificity component and chaperone

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Description (originally from EcoCyc[1]) ClpX ATP-dependent protease specificity component and chaperone

Comments (originally from EcoCyc[1]) ClpX is an ATP-dependent molecular chaperone that serves as a substrate-specifying adapter for the ClpP serine protease in the ClpXP and ClpAXP protease complexes.

ClpX protects the lambda O protein from heat-induced aggregation, disassembles lambda aggregates and enhances lambda DNA binding. ATP binding is required for all these effects, and disaggregation requires ATP hydrolysis [2][3][4][5][6][7][8][9][10][11][12][11][13][14][15][16][17][18][19][20][21].


References

  1. ↑ 1.0 1.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  2. ↑ Wawrzynow, A et al. (1995) The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone. EMBO J. 14 1867-77 PubMed
  3. ↑ Konieczny, I & Helinski, DR (1997) The replication initiation protein of the broad-host-range plasmid RK2 is activated by the ClpX chaperone. Proc. Natl. Acad. Sci. U.S.A. 94 14378-82 PubMed
  4. ↑ Mhammedi-Alaoui, A et al. (1994) A new component of bacteriophage Mu replicative transposition machinery: the Escherichia coli ClpX protein. Mol. Microbiol. 11 1109-16 PubMed
  5. ↑ Levchenko, I et al. (1995) Disassembly of the Mu transposase tetramer by the ClpX chaperone. Genes Dev. 9 2399-408 PubMed
  6. ↑ Kruklitis, R et al. (1996) ClpX protein of Escherichia coli activates bacteriophage Mu transposase in the strand transfer complex for initiation of Mu DNA synthesis. EMBO J. 15 935-44 PubMed
  7. ↑ Levchenko, I et al. (1997) ClpX and MuB interact with overlapping regions of Mu transposase: implications for control of the transposition pathway. Genes Dev. 11 1561-72 PubMed
  8. ↑ Wah, DA et al. (2002) Characterization of a specificity factor for an AAA+ ATPase: assembly of SspB dimers with ssrA-tagged proteins and the ClpX hexamer. Chem. Biol. 9 1237-45 PubMed
  9. ↑ Grimaud, R et al. (1998) Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP. J. Biol. Chem. 273 12476-81 PubMed
  10. ↑ Banecki, B et al. (2001) Structure-function analysis of the zinc-binding region of the Clpx molecular chaperone. J. Biol. Chem. 276 18843-8 PubMed
  11. ↑ 11.0 11.1 Singh, SK et al. (2001) Functional domains of the ClpA and ClpX molecular chaperones identified by limited proteolysis and deletion analysis. J. Biol. Chem. 276 29420-9 PubMed
  12. ↑ Kim, YI et al. (2001) Molecular determinants of complex formation between Clp/Hsp100 ATPases and the ClpP peptidase. Nat. Struct. Biol. 8 230-3 PubMed
  13. ↑ Joshi, SA et al. (2003) C-terminal domain mutations in ClpX uncouple substrate binding from an engagement step required for unfolding. Mol. Microbiol. 48 67-76 PubMed
  14. ↑ Hersch, GL et al. (2005) Asymmetric interactions of ATP with the AAA+ ClpX6 unfoldase: allosteric control of a protein machine. Cell 121 1017-27 PubMed
  15. ↑ Levchenko, I et al. (1997) PDZ-like domains mediate binding specificity in the Clp/Hsp100 family of chaperones and protease regulatory subunits. Cell 91 939-47 PubMed
  16. ↑ Smith, CK et al. (1999) Lon and Clp family proteases and chaperones share homologous substrate-recognition domains. Proc. Natl. Acad. Sci. U.S.A. 96 6678-82 PubMed
  17. ↑ Gottesman, S et al. (1993) ClpX, an alternative subunit for the ATP-dependent Clp protease of Escherichia coli. Sequence and in vivo activities. J. Biol. Chem. 268 22618-26 PubMed
  18. ↑ Donaldson, LW et al. (2003) Solution structure of the dimeric zinc binding domain of the chaperone ClpX. J. Biol. Chem. 278 48991-6 PubMed
  19. ↑ Weichart, D et al. (2003) Global role for ClpP-containing proteases in stationary-phase adaptation of Escherichia coli. J. Bacteriol. 185 115-25 PubMed
  20. ↑ Rajagopal, S et al. (2002) Sodium dodecyl sulfate hypersensitivity of clpP and clpB mutants of Escherichia coli. Appl. Environ. Microbiol. 68 4117-21 PubMed
  21. ↑ Yoo, SJ et al. (1994) clpX encoding an alternative ATP-binding subunit of protease Ti (Clp) can be expressed independently from clpP in Escherichia coli. Biochem. Biophys. Res. Commun. 203 798-804 PubMed

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