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Volumn 160, Issue 3, 2005, Pages 233-242

Salt stress induction of glutamyl endopeptidase biosynthesis in Bacillus intermedius

Author keywords

Biosynthesis; DegS DegU; Glutamyl endopeptidase; Salt stress; Serine protease

Indexed keywords

ENZYMES; GENES; PROTEINS; SODIUM CHLORIDE; STRESS ANALYSIS; SYNTHESIS (CHEMICAL);

EID: 20444420889     PISSN: 09445013     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.micres.2004.05.005     Document Type: Article
Times cited : (8)

References (33)
  • 1
    • 0027758497 scopus 로고
    • Extracellular alkaline proteinase from Bacillus intermedius. Isolation, purification and some properties of the enzyme
    • N.P. Balaban, M.R. Sharipova, A.M. Usmanova, E.L. Itskovitch, and I.B. Leshchinskaya Extracellular alkaline proteinase from Bacillus intermedius. Isolation, purification and some properties of the enzyme Biochemistry (Moscow) 58 1993 1923 1928
    • (1993) Biochemistry (Moscow) , vol.58 , pp. 1923-1928
    • Balaban, N.P.1    Sharipova, M.R.2    Usmanova, A.M.3    Itskovitch, E.L.4    Leshchinskaya, I.B.5
  • 3
    • 0031945892 scopus 로고    scopus 로고
    • Characterization of a novel member of the DegS-DegU regulon affected by salt stress in Bacillus subtilis
    • V. Dartois, M. Debarbouille, F. Kunst, and G. Rapoport Characterization of a novel member of the DegS-DegU regulon affected by salt stress in Bacillus subtilis J. Bacteriol. 180 1998 1855 1861
    • (1998) J. Bacteriol. , vol.180 , pp. 1855-1861
    • Dartois, V.1    Debarbouille, M.2    Kunst, F.3    Rapoport, G.4
  • 4
    • 0032622812 scopus 로고    scopus 로고
    • On the functional organization of glutamyl endopeptidases
    • I.V. Demidyuk, and S.V. Kostrov On the functional organization of glutamyl endopeptidases Mol. Biol. (Moscow) 33 1999 84 88
    • (1999) Mol. Biol. (Moscow) , vol.33 , pp. 84-88
    • Demidyuk, I.V.1    Kostrov, S.V.2
  • 5
    • 0029074510 scopus 로고
    • The ftsH gene of Bacillus subtilis is transiently induced after osmotic and temperature upshift
    • E. Deuerling, B. Paeslack, and W. Schuman The ftsH gene of Bacillus subtilis is transiently induced after osmotic and temperature upshift J. Bacteriol. 177 1995 4105 4112
    • (1995) J. Bacteriol. , vol.177 , pp. 4105-4112
    • Deuerling, E.1    Paeslack, B.2    Schuman, W.3
  • 6
    • 0015523789 scopus 로고
    • Purification and properties of an extracellular protease of Staphylococcus aureus
    • G. Drapeau, Y. Boily, and J. Houmard 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.1    Boily, Y.2    Houmard, J.3
  • 7
    • 0036786322 scopus 로고    scopus 로고
    • Distinct clpC genes control specific adaptive responses in Bacillus thuringiensis
    • S. Fedhila, T. Msadek, P. Nel, and D. Lereclus Distinct clpC genes control specific adaptive responses in Bacillus thuringiensis J. Bacteriol. 184 2002 5554 5562
    • (2002) J. Bacteriol. , vol.184 , pp. 5554-5562
    • Fedhila, S.1    Msadek, T.2    Nel, P.3    Lereclus, D.4
  • 9
    • 0037008375 scopus 로고    scopus 로고
    • Optimization of Bacillus intermedius glutamyl endopeptidase production by recombinant strain of Bacillus subtilis and localization of glutamyl endopeptidase in Bacillus subtilis cells
    • L.A. Gabdrakhmanova, N.P. Balaban, M.R. Sharipova, S.V. Kostrov, T.V. Akimkina, G.N. Rudenskaya, and I.B. Leshchinskaya Optimization of Bacillus intermedius glutamyl endopeptidase production by recombinant strain of Bacillus subtilis and localization of glutamyl endopeptidase in Bacillus subtilis cells Enzyme Microb. Technol. 31 2002 256 263
    • (2002) Enzyme Microb. Technol. , vol.31 , pp. 256-263
    • Gabdrakhmanova, L.A.1    Balaban, N.P.2    Sharipova, M.R.3    Kostrov, S.V.4    Akimkina, T.V.5    Rudenskaya, G.N.6    Leshchinskaya, I.B.7
  • 10
    • 0034987011 scopus 로고    scopus 로고
    • General stress response of Bacillus subtilis and other bacteria
    • M. Hecker, and U. Volker General stress response of Bacillus subtilis and other bacteria Adv. Microb. Physiol. 44 2001 35 91
    • (2001) Adv. Microb. Physiol. , vol.44 , pp. 35-91
    • Hecker, M.1    Volker, U.2
  • 11
    • 0029041524 scopus 로고
    • Compilation and analysis of Bacillus subtilis σa- dependent promoter sequences: Evidence for extended contact between RNA polymerase and upstream promoter DNA
    • J.D. Helmann Compilation and analysis of Bacillus subtilis σA-dependent promoter sequences: evidence for extended contact between RNA polymerase and upstream promoter DNA Nucl. Acids Res. 23 1995 2351 2360
    • (1995) Nucl. Acids Res. , vol.23 , pp. 2351-2360
    • Helmann, J.D.1
  • 14
    • 0026776211 scopus 로고
    • Positive regulation in the gram-positive bacterium Bacillus subtilis
    • A. Klier, T. Msadek, and G. Rapoport Positive regulation in the gram-positive bacterium Bacillus subtilis Annu. Rev. Microbiol. 46 1992 429 459
    • (1992) Annu. Rev. Microbiol. , vol.46 , pp. 429-459
    • Klier, A.1    Msadek, T.2    Rapoport, G.3
  • 15
    • 0029006115 scopus 로고
    • Salt stress is an environmental signal affecting degradative enzyme synthesis in Bacillus subtilis
    • F. Kunst, and G. Rapoport Salt stress is an environmental signal affecting degradative enzyme synthesis in Bacillus subtilis J. Bacteriol. 177 1995 2403 2407
    • (1995) J. Bacteriol. , vol.177 , pp. 2403-2407
    • Kunst, F.1    Rapoport, G.2
  • 17
    • 0036456146 scopus 로고    scopus 로고
    • Bacillus subtilis functional genomics: Genome-wide analysis of the DegS-DegU regulon by transcriptomics and proteomics
    • U. Mader, H. Antelmann, T. Buder, M.K. Dahl, M. Hecker, and G. Homuth Bacillus subtilis functional genomics: genome-wide analysis of the DegS-DegU regulon by transcriptomics and proteomics Mol. Genet. Genomics 268 2002 455 467
    • (2002) Mol. Genet. Genomics , vol.268 , pp. 455-467
    • Mader, U.1    Antelmann, H.2    Buder, T.3    Dahl, M.K.4    Hecker, M.5    Homuth, G.6
  • 18
    • 0034653286 scopus 로고    scopus 로고
    • Protein catabolism in growing Bacillus megaterium during adaptation to salt stress
    • D. Nekolny, and J. Chaloupka Protein catabolism in growing Bacillus megaterium during adaptation to salt stress FEMS Microbiol. Lett. 184 2000 173 177
    • (2000) FEMS Microbiol. Lett. , vol.184 , pp. 173-177
    • Nekolny, D.1    Chaloupka, J.2
  • 19
    • 0025633848 scopus 로고
    • Purification and characterization of an acidic amino acid-specific endopeptidase of Bacillus subtilis obtained from a commercial preparation (Protease Type XVI, Sigma)
    • T. Niidome, N. Yoshida, F. Ogata, A. Ido, and K. Noda Purification and characterization of an acidic amino acid-specific endopeptidase of Bacillus subtilis obtained from a commercial preparation (Protease Type XVI, Sigma) J. Biochem. (Tokyo) 108 1990 965 970
    • (1990) J. Biochem. (Tokyo) , vol.108 , pp. 965-970
    • Niidome, T.1    Yoshida, N.2    Ogata, F.3    Ido, A.4    Noda, K.5
  • 20
    • 0036377884 scopus 로고    scopus 로고
    • Characterization and molecular cloning of a glutamyl endopeptidase from Staphylococcus epidermidis
    • Y. Ohara-Nemoto, Y. Ikeda, M. Kobayashi, M. Sasaki, S. Tajika, and S. Kimura Characterization and molecular cloning of a glutamyl endopeptidase from Staphylococcus epidermidis Microb. Pathogen. 33 2002 33 41
    • (2002) Microb. Pathogen. , vol.33 , pp. 33-41
    • Ohara-Nemoto, Y.1    Ikeda, Y.2    Kobayashi, M.3    Sasaki, M.4    Tajika, S.5    Kimura, S.6
  • 23
    • 0345985794 scopus 로고    scopus 로고
    • Glutamylendopeptidases from microorganisms, a new subfamily of chymotrypsin proteases
    • G.N. Rudenskaya Glutamylendopeptidases from microorganisms, a new subfamily of chymotrypsin proteases Bioorg. Khim. (Moscow) 24 1998 256 261
    • (1998) Bioorg. Khim. (Moscow) , vol.24 , pp. 256-261
    • Rudenskaya, G.N.1
  • 27
    • 0036239754 scopus 로고    scopus 로고
    • Bacterial osmoadaptation: The role of osmolytes in bacterial stress and virulence
    • R.D. Sleator, and C. Hill Bacterial osmoadaptation: the role of osmolytes in bacterial stress and virulence FEMS Microbiol. Rev. 26 2001 49 71
    • (2001) FEMS Microbiol. Rev. , vol.26 , pp. 49-71
    • Sleator, R.D.1    Hill, C.2
  • 28
    • 0033659769 scopus 로고    scopus 로고
    • Control of sporulation initiation in Bacillus subtilis
    • A.L. Sonensein Control of sporulation initiation in Bacillus subtilis Curr. Opin. Microbiol. 3 2000 561 566
    • (2000) Curr. Opin. Microbiol. , vol.3 , pp. 561-566
    • Sonensein, A.L.1
  • 29
    • 0027506115 scopus 로고
    • Transition-state regulators: Sentinels of Bacillus subtilis post-exponential gene expression
    • M.A. Strauch, and J.A. Hoch Transition-state regulators: sentinels of Bacillus subtilis post-exponential gene expression Mol. Microbiol. 7 1993 337 342
    • (1993) Mol. Microbiol. , vol.7 , pp. 337-342
    • Strauch, M.A.1    Hoch, J.A.2
  • 30
    • 0026601661 scopus 로고
    • Isolation and amino acid sequence of a glutamic acid specific endopeptidase from Bacillus licheniformis
    • I. Svendsen, and K. Breddam Isolation and amino acid sequence of a glutamic acid specific endopeptidase from Bacillus licheniformis Eur. J. Biochem. 204 1992 165 171
    • (1992) Eur. J. Biochem. , vol.204 , pp. 165-171
    • Svendsen, I.1    Breddam, K.2
  • 31
    • 0032586856 scopus 로고    scopus 로고
    • Expression of the σb-dependent general stress regulon confers multiple stress resistance in Bacillus subtilis
    • U. Volker, B. Maul, and M. Hecker Expression of the σB- dependent general stress regulon confers multiple stress resistance in Bacillus subtilis J. Bacteriol. 181 1999 3942 3948
    • (1999) J. Bacteriol. , vol.181 , pp. 3942-3948
    • Volker, U.1    Maul, B.2    Hecker, M.3
  • 33
    • 0023678367 scopus 로고
    • Purification and characterization of an acidic amino acid specific endopeptidase of Streptomyces griseus obtained from a commercial preparation (Pronase)
    • N. Yoshida, S. Tsuruyama, K. Nagata, K. Hirayama, K. Noda, and S. Makisumi Purification and characterization of an acidic amino acid specific endopeptidase of Streptomyces griseus obtained from a commercial preparation (Pronase) J. Biochem. (Tokyo) 104 1988 451 456
    • (1988) J. Biochem. (Tokyo) , vol.104 , pp. 451-456
    • Yoshida, N.1    Tsuruyama, S.2    Nagata, K.3    Hirayama, K.4    Noda, K.5    Makisumi, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.