Category:Complex:serine protease Do
About
Description (originally from EcoCyc[1]) serine protease Do
Comments (originally from EcoCyc[1]) Protease Do, or DegP, is a periplasmic serine protease required for survival at high temperatures[2][3][4][5][3][6][7][8][9][10][11][12][13][14][15][16][17][8][18][19][20][21][22][23][24][22][25][8][26][27][2][28][29][23][30].
References
- ↑ 1.0 1.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ 2.0 2.1 Lipinska, B et al. (1989) Identification, characterization, and mapping of the Escherichia coli htrA gene, whose product is essential for bacterial growth only at elevated temperatures. J. Bacteriol. 171 1574-84 PubMed
- ↑ 3.0 3.1 Strauch, KL et al. (1989) Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature. J. Bacteriol. 171 2689-96 PubMed
- ↑ Seol, JH et al. (1991) Protease Do is essential for survival of Escherichia coli at high temperatures: its identity with the htrA gene product. Biochem. Biophys. Res. Commun. 176 730-6 PubMed
- ↑ Strauch, KL & Beckwith, J (1988) An Escherichia coli mutation preventing degradation of abnormal periplasmic proteins. Proc. Natl. Acad. Sci. U.S.A. 85 1576-80 PubMed
- ↑ Skórko-Glonek, J et al. (1999) The Escherichia coli heat shock protease HtrA participates in defense against oxidative stress. Mol. Gen. Genet. 262 342-50 PubMed
- ↑ 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
- ↑ 8.0 8.1 8.2 Spiess, C et al. (1999) A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell 97 339-47 PubMed
- ↑ Kihara, A & Ito, K (1998) Translocation, folding, and stability of the HflKC complex with signal anchor topogenic sequences. J. Biol. Chem. 273 29770-5 PubMed
- ↑ Misra, R et al. (1991) A genetic approach for analyzing the pathway of LamB assembly into the outer membrane of Escherichia coli. J. Biol. Chem. 266 13592-7 PubMed
- ↑ Jones, CH et al. (2002) Escherichia coli DegP protease cleaves between paired hydrophobic residues in a natural substrate: the PapA pilin. J. Bacteriol. 184 5762-71 PubMed
- ↑ Lee, CS et al. (1990) Processing of Ada protein by two serine endoproteases Do and So from Escherichia coli. FEBS Lett. 262 310-2 PubMed
- ↑ Cavard, D et al. (1989) The acylated precursor form of the colicin A lysis protein is a natural substrate of the DegP protease. J. Bacteriol. 171 6316-22 PubMed
- ↑ Cavard, D (1995) Role of DegP protease on levels of various forms of colicin A lysis protein. FEMS Microbiol. Lett. 125 173-8 PubMed
- ↑ Yoo, SJ et al. (1993) Hydrolysis of the IciA protein, an inhibitor of DNA replication initiation, by protease Do in Escherichia coli. FEBS Lett. 327 17-20 PubMed
- ↑ Spiers, A et al. (2002) PDZ domains facilitate binding of high temperature requirement protease A (HtrA) and tail-specific protease (Tsp) to heterologous substrates through recognition of the small stable RNA A (ssrA)-encoded peptide. J. Biol. Chem. 277 39443-9 PubMed
- ↑ Ulvatne, H et al. (2002) Proteases in Escherichia coli and Staphylococcus aureus confer reduced susceptibility to lactoferricin B. J. Antimicrob. Chemother. 50 461-7 PubMed
- ↑ Misra, R et al. (2000) Overexpression of protease-deficient DegP(S210A) rescues the lethal phenotype of Escherichia coli OmpF assembly mutants in a degP background. J. Bacteriol. 182 4882-8 PubMed
- ↑ Rizzitello, AE et al. (2001) Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli. J. Bacteriol. 183 6794-800 PubMed
- ↑ Swamy, KH et al. (1983) Isolation and characterization of protease do from Escherichia coli, a large serine protease containing multiple subunits. Arch. Biochem. Biophys. 224 543-54 PubMed
- ↑ Kim, KI et al. (1999) Selective degradation of unfolded proteins by the self-compartmentalizing HtrA protease, a periplasmic heat shock protein in Escherichia coli. J. Mol. Biol. 294 1363-74 PubMed
- ↑ 22.0 22.1 Krojer, T et al. (2002) Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine. Nature 416 455-9 PubMed
- ↑ 23.0 23.1 Sassoon, N et al. (1999) PDZ domains determine the native oligomeric structure of the DegP (HtrA) protease. Mol. Microbiol. 33 583-9 PubMed
- ↑ Iwanczyk, J et al. (2007) Role of the PDZ domains in Escherichia coli DegP protein. J. Bacteriol. 189 3176-86 PubMed
- ↑ Skórko-Glonek, J et al. (1995) Comparison of the structure of wild-type HtrA heat shock protease and mutant HtrA proteins. A Fourier transform infrared spectroscopic study. J. Biol. Chem. 270 11140-6 PubMed
- ↑ Skórko-Glonek, J et al. (1997) HtrA heat shock protease interacts with phospholipid membranes and undergoes conformational changes. J. Biol. Chem. 272 8974-82 PubMed
- ↑ Lipinska, B et al. (1990) The HtrA (DegP) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase. J. Bacteriol. 172 1791-7 PubMed
- ↑ Baars, L et al. (2006) Defining the role of the Escherichia coli chaperone SecB using comparative proteomics. J. Biol. Chem. 281 10024-34 PubMed
- ↑ Ponting, CP (1997) Evidence for PDZ domains in bacteria, yeast, and plants. Protein Sci. 6 464-8 PubMed
- ↑ Forns, N et al. (2005) Osmoregulation of the HtrA (DegP) protease of Escherichia coli: an Hha-H-NS complex represses HtrA expression at low osmolarity. FEMS Microbiol. Lett. 251 75-80 PubMed
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