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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 EcoliWiki page
  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 EcoliWiki page
  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 EcoliWiki page
  5. ↑ Levchenko I et al. (1995) Disassembly of the Mu transposase tetramer by the ClpX chaperone. Genes Dev 9: 2399-408 PubMed EcoliWiki page
  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 EcoliWiki page
  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 EcoliWiki page
  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 EcoliWiki page
  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 EcoliWiki page
  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 EcoliWiki page
  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 EcoliWiki page
  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 EcoliWiki page
  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 EcoliWiki page
  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 EcoliWiki page
  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 EcoliWiki page
  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 EcoliWiki page
  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 EcoliWiki page
  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 EcoliWiki page
  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 EcoliWiki page
  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 EcoliWiki page
  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 EcoliWiki page

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