Category:Complex:DNA-binding, ATP-dependent protease La

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Description (originally from EcoCyc[1]) DNA-binding, ATP-dependent protease La

Comments (originally from EcoCyc[1]) Lon is an ATP-dependent protease responsible for degradation of misfolded proteins as well as a number of rapidly degraded regulatory proteins. Key regulatory proteins that are Lon substrates include the cell division regulator SulA [2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20][21][20][22][23][24][25][26][27][28][29][28][30][31][32][33][34][35][36][27][37][33][23][27][38][39][40][41][42][26].


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. ↑ Schoemaker, JM et al. (1984) Regulation of cell division in Escherichia coli: SOS induction and cellular location of the sulA protein, a key to lon-associated filamentation and death. J Bacteriol 158 551-61 PubMed
  3. ↑ Higashitani, A et al. (1997) Functional dissection of a cell-division inhibitor, SulA, of Escherichia coli and its negative regulation by Lon. Mol Gen Genet 254 351-7 PubMed
  4. ↑ Torres-Cabassa, AS & Gottesman, S (1987) Capsule synthesis in Escherichia coli K-12 is regulated by proteolysis. J Bacteriol 169 981-9 PubMed
  5. ↑ Dopazo, A et al. (1987) Structural inhibition and reactivation of Escherichia coli septation by elements of the SOS and TER pathways. J Bacteriol 169 1772-6 PubMed
  6. ↑ Chung, CH & Goldberg, AL (1981) The product of the lon (capR) gene in Escherichia coli is the ATP-dependent protease, protease La. Proc. Natl. Acad. Sci. U.S.A. 78 4931-5 PubMed
  7. ↑ Ryzhavskaia, AS et al. (1988) [Stability of normal, abnormal and recombinant proteins in Escherichia coli strains deficient for intracellular proteinase La--the product of the lon gene]. Mol Biol (Mosk) 22 201-8 PubMed
  8. ↑ Laskowska, E et al. (1996) Degradation by proteases Lon, Clp and HtrA, of Escherichia coli proteins aggregated in vivo by heat shock; HtrA protease action in vivo and in vitro. Mol. Microbiol. 22 555-71 PubMed
  9. ↑ Rosen, R et al. (2002) Protein aggregation in Escherichia coli: role of proteases. FEMS Microbiol. Lett. 207 9-12 PubMed
  10. ↑ Sherman MYu, & Goldberg, AL (1992) Involvement of the chaperonin dnaK in the rapid degradation of a mutant protein in Escherichia coli. EMBO J 11 71-7 PubMed
  11. ↑ Maurizi, MR (1987) Degradation in vitro of bacteriophage lambda N protein by Lon protease from Escherichia coli. J Biol Chem 262 2696-703 PubMed
  12. ↑ Leffers, GG Jr & Gottesman, S (1998) Lambda Xis degradation in vivo by Lon and FtsH. J Bacteriol 180 1573-7 PubMed
  13. ↑ Bonnefoy, E et al. (1989) Lon-dependent regulation of the DNA binding protein HU in Escherichia coli. Proc Natl Acad Sci U S A 86 7691-5 PubMed
  14. ↑ Wang, L et al. (1999) Conditional stability of the HemA protein (glutamyl-tRNA reductase) regulates heme biosynthesis in Salmonella typhimurium. J. Bacteriol. 181 1211-9 PubMed
  15. ↑ Calmann, MA & Marinus, MG (2003) Regulated expression of the Escherichia coli dam gene. J Bacteriol 185 5012-4 PubMed
  16. ↑ Van Melderen, L et al. (1996) ATP-dependent degradation of CcdA by Lon protease. Effects of secondary structure and heterologous subunit interactions. J Biol Chem 271 27730-8 PubMed
  17. ↑ Van Melderen, L et al. (1994) Lon-dependent proteolysis of CcdA is the key control for activation of CcdB in plasmid-free segregant bacteria. Mol Microbiol 11 1151-7 PubMed
  18. ↑ Grønlund, H & Gerdes, K (1999) Toxin-antitoxin systems homologous with relBE of Escherichia coli plasmid P307 are ubiquitous in prokaryotes. J Mol Biol 285 1401-15 PubMed
  19. ↑ Smith, AS & Rawlings, DE (1998) Efficiency of the pTF-FC2 pas poison-antidote stability system in Escherichia coli is affected by the host strain, and antidote degradation requires the lon protease. J Bacteriol 180 5458-62 PubMed
  20. ↑ 20.0 20.1 Christensen, SK et al. (2001) RelE, a global inhibitor of translation, is activated during nutritional stress. Proc Natl Acad Sci U S A 98 14328-33 PubMed
  21. ↑ Christensen, SK et al. (2004) Overproduction of the Lon protease triggers inhibition of translation in Escherichia coli: involvement of the yefM-yoeB toxin-antitoxin system. Mol. Microbiol. 51 1705-17 PubMed
  22. ↑ Christensen, SK et al. (2003) Toxin-antitoxin loci as stress-response-elements: ChpAK/MazF and ChpBK cleave translated RNAs and are counteracted by tmRNA. J. Mol. Biol. 332 809-19 PubMed
  23. ↑ 23.0 23.1 Charette, MF et al. (1981) ATP hydrolysis-dependent protease activity of the lon (capR) protein of Escherichia coli K-12. Proc. Natl. Acad. Sci. U.S.A. 78 4728-32 PubMed
  24. ↑ Waxman, L & Goldberg, AL (1985) Protease La, the lon gene product, cleaves specific fluorogenic peptides in an ATP-dependent reaction. J Biol Chem 260 12022-8 PubMed
  25. ↑ Botos, I et al. (2004) The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site. J. Biol. Chem. 279 8140-8 PubMed
  26. ↑ 26.0 26.1 Nishii, W et al. (2005) Cleavage mechanism of ATP-dependent Lon protease toward ribosomal S2 protein. FEBS Lett 579 6846-50 PubMed
  27. ↑ 27.0 27.1 27.2 Chin, DT et al. (1988) Sequence of the lon gene in Escherichia coli. A heat-shock gene which encodes the ATP-dependent protease La. J Biol Chem 263 11718-28 PubMed
  28. ↑ 28.0 28.1 Menon, AS & Goldberg, AL (1987) Binding of nucleotides to the ATP-dependent protease La from Escherichia coli. J. Biol. Chem. 262 14921-8 PubMed
  29. ↑ Vineyard, D et al. (2006) Transient kinetic experiments demonstrate the existence of a unique catalytic enzyme form in the peptide-stimulated ATPase mechanism of Escherichia coli Lon protease. Biochemistry 45 11432-43 PubMed
  30. ↑ Menon, AS et al. (1987) The energy utilized in protein breakdown by the ATP-dependent protease (La) from Escherichia coli. J Biol Chem 262 722-6 PubMed
  31. ↑ Fischer, H & Glockshuber, R (1994) A point mutation within the ATP-binding site inactivates both catalytic functions of the ATP-dependent protease La (Lon) from Escherichia coli. FEBS Lett 356 101-3 PubMed
  32. ↑ Waxman, L & Goldberg, AL (1982) Protease La from Escherichia coli hydrolyzes ATP and proteins in a linked fashion. Proc Natl Acad Sci U S A 79 4883-7 PubMed
  33. ↑ 33.0 33.1 Pohl, A et al. (1976) [Glutathione reductase deficiency with membrane defect in hereditary hemolytic anemia]. Acta Haematol 56 47-57 PubMed
  34. ↑ Goldberg, AL & Waxman, L (1985) The role of ATP hydrolysis in the breakdown of proteins and peptides by protease La from Escherichia coli. J Biol Chem 260 12029-34 PubMed
  35. ↑ Rasulova, FS et al. (1998) The isolated proteolytic domain of Escherichia coli ATP-dependent protease Lon exhibits the peptidase activity. FEBS Lett. 432 179-81 PubMed
  36. ↑ Vasilyeva, OV et al. (2002) Domain structure and ATP-induced conformational changes in Escherichia coli protease Lon revealed by limited proteolysis and autolysis. FEBS Lett 526 66-70 PubMed
  37. ↑ Waxman, L & Goldberg, AL (1986) Selectivity of intracellular proteolysis: protein substrates activate the ATP-dependent protease (La). Science 232 500-3 PubMed
  38. ↑ Chung, CH & Goldberg, AL (1982) DNA stimulates ATP-dependent proteolysis and protein-dependent ATPase activity of protease La from Escherichia coli. Proc Natl Acad Sci U S A 79 795-9 PubMed
  39. ↑ Charette, MF et al. (1984) DNA-stimulated ATPase activity on the lon (CapR) protein. J Bacteriol 158 195-201 PubMed
  40. ↑ Fu, GK et al. (1997) Bacterial protease Lon is a site-specific DNA-binding protein. J. Biol. Chem. 272 534-8 PubMed
  41. ↑ Kuroda, A et al. (2001) Role of inorganic polyphosphate in promoting ribosomal protein degradation by the Lon protease in E. coli. Science 293 705-8 PubMed
  42. ↑ Nomura, K et al. (2004) Effects of inorganic polyphosphate on the proteolytic and DNA-binding activities of Lon in Escherichia coli. J Biol Chem 279 34406-10 PubMed

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