메뉴 건너뛰기




Volumn 381, Issue 1, 2008, Pages 74-80

An Escherichia coli expression system for glutamyl endopeptidases optimized by complete suppression of autodegradation

Author keywords

Autoproteolysis; Glutamyl endopeptidase; Prosequence; Staphylococcus epidermidis; Staphylococcus warneri

Indexed keywords

ESCHERICHIA COLI; RECOMBINANT PROTEINS; SOAPS (DETERGENTS);

EID: 49049084197     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2008.06.022     Document Type: Article
Times cited : (9)

References (20)
  • 1
    • 0015523789 scopus 로고
    • Purification and properties of an extracellular protease of Staphylococcus aureus
    • Drapeau G.R., Boily Y., and Houmard J. Purification and properties of an extracellular protease of Staphylococcus aureus. J. Biol. Chem. 247 (1972) 6720-6726
    • (1972) J. Biol. Chem. , vol.247 , pp. 6720-6726
    • Drapeau, G.R.1    Boily, Y.2    Houmard, J.3
  • 3
    • 0034917099 scopus 로고    scopus 로고
    • Decreased amounts of cell wall-associated protein A and fibronectin-binding proteins in Staphylococcus aureus sarA mutants due to up-regulation of extracellular proteases
    • Karlsson A., Saravia-Otten P., Tegmark K., Morfeldt E., and Arvidson S. Decreased amounts of cell wall-associated protein A and fibronectin-binding proteins in Staphylococcus aureus sarA mutants due to up-regulation of extracellular proteases. Infect. Immun. 69 (2001) 4742-4748
    • (2001) Infect. Immun. , vol.69 , pp. 4742-4748
    • Karlsson, A.1    Saravia-Otten, P.2    Tegmark, K.3    Morfeldt, E.4    Arvidson, S.5
  • 4
    • 0002333481 scopus 로고    scopus 로고
    • Glutamyl endopeptidase I
    • Barrett A.J., Rawlings N.D., and Woessner Jr. F.F. (Eds), Academic Press, San Diego
    • Stennicke H.R., and Breddam K. Glutamyl endopeptidase I. In: Barrett A.J., Rawlings N.D., and Woessner Jr. F.F. (Eds). Handbook of Proteolytic Enzymes (1998), Academic Press, San Diego 243-246
    • (1998) Handbook of Proteolytic Enzymes , pp. 243-246
    • Stennicke, H.R.1    Breddam, K.2
  • 5
    • 0023664778 scopus 로고
    • Nucleotide sequence of the serine protease gene of Staphylococcus aureus, strain V8
    • Carmona C., and Gray G.L. Nucleotide sequence of the serine protease gene of Staphylococcus aureus, strain V8. Nucleic Acids Res. 15 (1987) 6757
    • (1987) Nucleic Acids Res. , vol.15 , pp. 6757
    • Carmona, C.1    Gray, G.L.2
  • 6
    • 0018082649 scopus 로고
    • Role of a metalloprotease in activation of the precursor of staphylococcal protease
    • Drapeau G.R. Role of a metalloprotease in activation of the precursor of staphylococcal protease. J. Bacteriol. 136 (1978) 607-613
    • (1978) J. Bacteriol. , vol.136 , pp. 607-613
    • Drapeau, G.R.1
  • 7
    • 14244266586 scopus 로고    scopus 로고
    • Cytoplasmic control of premature activation of a secreted protease zymogen: Deletion of staphostatin B (SspC) in Staphylococcus aureus 8325-4 yields a profound pleiotropic phenotype
    • Shaw L.N., Golonka E., Szmyd G., Foster S.J., Travis J., and Potempa J. Cytoplasmic control of premature activation of a secreted protease zymogen: Deletion of staphostatin B (SspC) in Staphylococcus aureus 8325-4 yields a profound pleiotropic phenotype. J. Bacteriol. 187 (2005) 1751-1762
    • (2005) J. Bacteriol. , vol.187 , pp. 1751-1762
    • Shaw, L.N.1    Golonka, E.2    Szmyd, G.3    Foster, S.J.4    Travis, J.5    Potempa, J.6
  • 9
    • 0036377884 scopus 로고    scopus 로고
    • Characterization and molecular cloning of a glutamyl endopeptidase from Staphylococcus epidermidis
    • Ohara-Nemoto Y., Ikeda Y., Kobayashi M., Sasaki M., Tajika S., and Kimura S. Characterization and molecular cloning of a glutamyl endopeptidase from Staphylococcus epidermidis. Microb. Pathog. 33 (2002) 33-41
    • (2002) Microb. Pathog. , vol.33 , pp. 33-41
    • Ohara-Nemoto, Y.1    Ikeda, Y.2    Kobayashi, M.3    Sasaki, M.4    Tajika, S.5    Kimura, S.6
  • 11
    • 0028812611 scopus 로고
    • Hyperproduction of a recombinant fusion protein of Staphylococcus aureus V8 protease in Escherichia coli and its processing by OmpT protease to release an active V8 protease derivative
    • Yabuta M., Ochi N., and Ohsuye K. Hyperproduction of a recombinant fusion protein of Staphylococcus aureus V8 protease in Escherichia coli and its processing by OmpT protease to release an active V8 protease derivative. Appl. Microbiol. Biotechnol. 44 (1995) 118-125
    • (1995) Appl. Microbiol. Biotechnol. , vol.44 , pp. 118-125
    • Yabuta, M.1    Ochi, N.2    Ohsuye, K.3
  • 12
    • 36349012610 scopus 로고    scopus 로고
    • Activation of the SspA serine protease zymogen of Staphylococcus aureus proceeds through unique variations of a trypsinogen-like mechanism and is dependent on both autocatalytic and metalloprotease-specific processing
    • Nickerson N.N., Prasad L., Jacob L., Delbaere L.T., and McGavin M.J. Activation of the SspA serine protease zymogen of Staphylococcus aureus proceeds through unique variations of a trypsinogen-like mechanism and is dependent on both autocatalytic and metalloprotease-specific processing. J. Biol. Chem. 282 (2007) 34129-34138
    • (2007) J. Biol. Chem. , vol.282 , pp. 34129-34138
    • Nickerson, N.N.1    Prasad, L.2    Jacob, L.3    Delbaere, L.T.4    McGavin, M.J.5
  • 13
    • 38149018614 scopus 로고    scopus 로고
    • Characterization of the glutamyl endopeptidase from Staphylococcus aureus expressed in Escherichia coli
    • Nemoto T.K., Ohara-Nemoto Y., Ono T., Kobayakawa T., Shimoyama Y., Kimura S., and Takagi T. Characterization of the glutamyl endopeptidase from Staphylococcus aureus expressed in Escherichia coli. FEBS J. 275 (2008) 573-587
    • (2008) FEBS J. , vol.275 , pp. 573-587
    • Nemoto, T.K.1    Ohara-Nemoto, Y.2    Ono, T.3    Kobayakawa, T.4    Shimoyama, Y.5    Kimura, S.6    Takagi, T.7
  • 14
    • 49049109163 scopus 로고    scopus 로고
    • Y. Ohara-Nemoto, T. Ono, Y. Shimoyama, S. Kimura, T. K. Nemoto, Homologous and heterologous expression and maturation processing of extracellular glutamyl endopeptidase of Staphylococcus epidermidis, Biol. Chem. (in press).
    • Y. Ohara-Nemoto, T. Ono, Y. Shimoyama, S. Kimura, T. K. Nemoto, Homologous and heterologous expression and maturation processing of extracellular glutamyl endopeptidase of Staphylococcus epidermidis, Biol. Chem. (in press).
  • 15
    • 6344275668 scopus 로고    scopus 로고
    • PCR-based identification of Staphylococcus epidermidis targeting gseA encoding the glutamic-acid-specific protease
    • Ikeda Y., Ohara-Nemoto Y., Kimura S., Ishibashi K., and Kikuchi K. PCR-based identification of Staphylococcus epidermidis targeting gseA encoding the glutamic-acid-specific protease. Can. J. Microbiol. 50 (2004) 493-498
    • (2004) Can. J. Microbiol. , vol.50 , pp. 493-498
    • Ikeda, Y.1    Ohara-Nemoto, Y.2    Kimura, S.3    Ishibashi, K.4    Kikuchi, K.5
  • 16
    • 2942623769 scopus 로고    scopus 로고
    • The region adjacent to the highly immunogenic site and shielded by the middle domain is responsible for self-oligomerization/client binding of HSP90 molecular chaperone
    • Nemoto T.K., Fukuma Y., Yamada S., Kobayakawa T., Ono T., and Ohara-Nemoto Y. The region adjacent to the highly immunogenic site and shielded by the middle domain is responsible for self-oligomerization/client binding of HSP90 molecular chaperone. Biochemistry 43 (2004) 7628-7636
    • (2004) Biochemistry , vol.43 , pp. 7628-7636
    • Nemoto, T.K.1    Fukuma, Y.2    Yamada, S.3    Kobayakawa, T.4    Ono, T.5    Ohara-Nemoto, Y.6
  • 17
    • 11144333056 scopus 로고    scopus 로고
    • Molecular diversity of a putative virulence factor: Purification and characterization of isoforms of an extracellular serine glutamyl endopeptidase of Enterococcus faecalis with different enzymatic activities
    • Kawalec M., Potempa J., Moon J.L., Travis J., and Murray B.E. Molecular diversity of a putative virulence factor: Purification and characterization of isoforms of an extracellular serine glutamyl endopeptidase of Enterococcus faecalis with different enzymatic activities. J. Bacteriol. 187 (2005) 266-275
    • (2005) J. Bacteriol. , vol.187 , pp. 266-275
    • Kawalec, M.1    Potempa, J.2    Moon, J.L.3    Travis, J.4    Murray, B.E.5
  • 18
    • 0026503259 scopus 로고
    • Substrate preference of glutamic-acid-specific endopeptidases assessed by synthetic peptide substrates based on intramolecular fluorescences quenching
    • Breddam K., and Mendal M. Substrate preference of glutamic-acid-specific endopeptidases assessed by synthetic peptide substrates based on intramolecular fluorescences quenching. Eur. J. Biochem. 206 (1992) 103-107
    • (1992) Eur. J. Biochem. , vol.206 , pp. 103-107
    • Breddam, K.1    Mendal, M.2
  • 19
    • 14644437656 scopus 로고    scopus 로고
    • Folding pathway mediated by an intramolecular chaperone: Intrinsically unstructured propeptide modulates stochastic activation of subtilisin
    • Subbian E., Yabuta Y., and Shinde U.P. Folding pathway mediated by an intramolecular chaperone: Intrinsically unstructured propeptide modulates stochastic activation of subtilisin. J. Mol. Biol. 347 (2005) 367-383
    • (2005) J. Mol. Biol. , vol.347 , pp. 367-383
    • Subbian, E.1    Yabuta, Y.2    Shinde, U.P.3
  • 20
    • 4644234235 scopus 로고    scopus 로고
    • The structure of a universally employed enzyme: V8 protease from Staphylococcus aureus
    • Prasad L., Leduc Y., Hayakawa K., and Delbaere L.T. The structure of a universally employed enzyme: V8 protease from Staphylococcus aureus. Acta Crystallogr. 60 (2004) 256-259
    • (2004) Acta Crystallogr. , vol.60 , pp. 256-259
    • Prasad, L.1    Leduc, Y.2    Hayakawa, K.3    Delbaere, L.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.