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Volumn 79, Issue 6, 1997, Pages 315-322

Artefactual cleavage of E coli H-NS by OmpT

Author keywords

Escherichia coli; H NS; Histone; OmpT; Protease

Indexed keywords

DNA BINDING PROTEIN; OUTER MEMBRANE PROTEIN;

EID: 0030827925     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9084(97)80025-9     Document Type: Article
Times cited : (7)

References (39)
  • 3
    • 0025961415 scopus 로고
    • Osmotic signal transduction to proU is independent of DNA supercoiling in Escherichia coli
    • Ramirez RM, Villarejo M (1991 ) Osmotic signal transduction to proU is independent of DNA supercoiling in Escherichia coli, J Bacteriol 173, 879-885
    • (1991) J Bacteriol , vol.173 , pp. 879-885
    • Ramirez, R.M.1    Villarejo, M.2
  • 4
    • 0025359664 scopus 로고
    • Sequence determinants for H1 binding on Escherichia coli lac and gal promoters
    • Rimsky S, Spassky A (1990) Sequence determinants for H1 binding on Escherichia coli lac and gal promoters. Biochemistry 29, 3765-3771
    • (1990) Biochemistry , vol.29 , pp. 3765-3771
    • Rimsky, S.1    Spassky, A.2
  • 5
    • 0025003429 scopus 로고
    • An Escherichia coli protein that preferentially binds to sharply curved DNA
    • Yamada H, Muramatsu S, Mizuno T (1990) An Escherichia coli protein that preferentially binds to sharply curved DNA. J Biochem 108, 420-425
    • (1990) J Biochem , vol.108 , pp. 420-425
    • Yamada, H.1    Muramatsu, S.2    Mizuno, T.3
  • 6
    • 0025909704 scopus 로고
    • Systematic characterization of curved DNA segments randomly cloned from Escherichia coli and their functional significance
    • Tanaka KI, Muramatsu S, Yamada H, Mizuno T (1991) Systematic characterization of curved DNA segments randomly cloned from Escherichia coli and their functional significance. Mol Gen Genet 226, 367-376
    • (1991) Mol Gen Genet , vol.226 , pp. 367-376
    • Tanaka, K.I.1    Muramatsu, S.2    Yamada, H.3    Mizuno, T.4
  • 7
    • 0028285269 scopus 로고
    • Interactions of the nucleoid-associated DNA-binding protein H-NS with the regulatory region of the osmotically controlled proU operon of Escherichia coli
    • Lucht JM, Dersch P, Kempf B, Bremer E (1994) Interactions of the nucleoid-associated DNA-binding protein H-NS with the regulatory region of the osmotically controlled proU operon of Escherichia coli. J Biol Chem 269, 6578-6586
    • (1994) J Biol Chem , vol.269 , pp. 6578-6586
    • Lucht, J.M.1    Dersch, P.2    Kempf, B.3    Bremer, E.4
  • 9
    • 0027408394 scopus 로고
    • The Escherichia coli nucleoid protein H-NS functions directly as a transcriptional repressor
    • Ueguchi C, Mizuno T (1993) The Escherichia coli nucleoid protein H-NS functions directly as a transcriptional repressor. EMBO J 12, 1039-1046
    • (1993) EMBO J , vol.12 , pp. 1039-1046
    • Ueguchi, C.1    Mizuno, T.2
  • 10
    • 0027500211 scopus 로고
    • Autoregulatory expression of the Escherichia coli hns gene encoding a nucleoid protein: H-NS functions as a repressor of its own expression
    • Ueguchi C, Kakeda M, Mizuno T (1993) Autoregulatory expression of the Escherichia coli hns gene encoding a nucleoid protein: H-NS functions as a repressor of its own expression. Mol Gen Genet 236, 171-178
    • (1993) Mol Gen Genet , vol.236 , pp. 171-178
    • Ueguchi, C.1    Kakeda, M.2    Mizuno, T.3
  • 11
    • 0015441270 scopus 로고
    • Two heat-resistant, low molecular weight proteins from Escherichia coli that stimulate DNA-directed RNA synthesis
    • Cukier-Kahn R, Jacquet M, Gros F (1972) Two heat-resistant, low molecular weight proteins from Escherichia coli that stimulate DNA-directed RNA synthesis. Proc Natl Acad Sci USA 69, 3643-3647
    • (1972) Proc Natl Acad Sci USA , vol.69 , pp. 3643-3647
    • Cukier-Kahn, R.1    Jacquet, M.2    Gros, F.3
  • 12
    • 0021760528 scopus 로고
    • H1a, an E coli DNA binding protein which accumulates in stationary phase, strongly compacts DNA in vitro
    • Spassky A, Rimsky S, Garreau H, Buc H (1984) H1a, an E coli DNA binding protein which accumulates in stationary phase, strongly compacts DNA in vitro. Nucleic Acids Res 12, 5321-5340
    • (1984) Nucleic Acids Res , vol.12 , pp. 5321-5340
    • Spassky, A.1    Rimsky, S.2    Garreau, H.3    Buc, H.4
  • 14
    • 0025968977 scopus 로고
    • DNA supercoiling and environmental regulation of gene expression in pathogenic bacteria
    • Dorman CJ (1991) DNA supercoiling and environmental regulation of gene expression in pathogenic bacteria. Infect Immun 59, 745-749
    • (1991) Infect Immun , vol.59 , pp. 745-749
    • Dorman, C.J.1
  • 15
    • 0026454716 scopus 로고
    • Regulation by proteolysis: Energy-dependent proteases and their targets
    • Gottesman S, Maurizi MR (1992) Regulation by proteolysis: energy-dependent proteases and their targets. Microbiol Rev 56, 592-621
    • (1992) Microbiol Rev , vol.56 , pp. 592-621
    • Gottesman, S.1    Maurizi, M.R.2
  • 16
    • 0029044486 scopus 로고
    • Anucleate cell production by Escherichia coli Dhns mutant lacking a histone-like protein, H-NS
    • Kaidow A, Wachi M, Nakamura J, Magae J, Nagai K (1995) Anucleate cell production by Escherichia coli Dhns mutant lacking a histone-like protein, H-NS. J Bacteriol 177, 3589-3592
    • (1995) J Bacteriol , vol.177 , pp. 3589-3592
    • Kaidow, A.1    Wachi, M.2    Nakamura, J.3    Magae, J.4    Nagai, K.5
  • 17
    • 0025357506 scopus 로고
    • SecY protein, a membrane-embedded secretion factor of E coli, is cleaved by the OmpT protease in vitro
    • Akiyama Y, Ito K (1990) SecY protein, a membrane-embedded secretion factor of E coli, is cleaved by the OmpT protease in vitro. Biochem Biophys Res Commun 167, 711-715
    • (1990) Biochem Biophys Res Commun , vol.167 , pp. 711-715
    • Akiyama, Y.1    Ito, K.2
  • 18
    • 0025057970 scopus 로고
    • In vivo degradation of secreted fusion proteins by the Escherichia coli outer membrane protease OmpT
    • Baneyx F, Georgiou G (1990) In vivo degradation of secreted fusion proteins by the Escherichia coli outer membrane protease OmpT. J Bacteriol 172, 491-494
    • (1990) J Bacteriol , vol.172 , pp. 491-494
    • Baneyx, F.1    Georgiou, G.2
  • 19
    • 0028082052 scopus 로고
    • Artefactual processing of penicillin-binding proteins 7 and 1b by the OmpT protease of Escherichia coli
    • Henderson TA, Dombrosky PM, Young KE (1994) Artefactual processing of penicillin-binding proteins 7 and 1b by the OmpT protease of Escherichia coli. J Bacteriol 176, 256-259
    • (1994) J Bacteriol , vol.176 , pp. 256-259
    • Henderson, T.A.1    Dombrosky, P.M.2    Young, K.E.3
  • 20
    • 0017129243 scopus 로고
    • Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu
    • Casadaban MJ (1976) Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu. J Mol Biol 104, 514-555
    • (1976) J Mol Biol , vol.104 , pp. 514-555
    • Casadaban, M.J.1
  • 22
    • 0017640242 scopus 로고
    • The transposon Tn1 as a probe for studying ColE1 structure and function
    • Dougan G, Sherrat D (1977) The transposon Tn1 as a probe for studying ColE1 structure and function. Mol Gen Genet 151, 151-160
    • (1977) Mol Gen Genet , vol.151 , pp. 151-160
    • Dougan, G.1    Sherrat, D.2
  • 23
    • 0015318675 scopus 로고
    • Membrane mutation associated with sensitivity to acriflavine in Escherichia coli
    • Nakamura H, Sugunuma A (1972) Membrane mutation associated with sensitivity to acriflavine in Escherichia coli. J Bacteriol 110, 329-335
    • (1972) J Bacteriol , vol.110 , pp. 329-335
    • Nakamura, H.1    Sugunuma, A.2
  • 24
    • 0020418554 scopus 로고
    • Versatile low-copy number plasmid vectors for cloning in Escherichia coli
    • Stoker NG, Fairweather NF, Spratt BG (1982) Versatile low-copy number plasmid vectors for cloning in Escherichia coli. Gene 18, 335-341
    • (1982) Gene , vol.18 , pp. 335-341
    • Stoker, N.G.1    Fairweather, N.F.2    Spratt, B.G.3
  • 25
    • 0021154990 scopus 로고
    • Review article. Immunoblotting and dot immunoblotting
    • Towbin H, Gordon J (1984) Review article. Immunoblotting and dot immunoblotting. J Immunol Methods 72, 313-340
    • (1984) J Immunol Methods , vol.72 , pp. 313-340
    • Towbin, H.1    Gordon, J.2
  • 26
    • 39049174255 scopus 로고
    • Enzyme-labelled antibodies: Preparation and application for the localization of antigens
    • Nakane PK, Pierce GB (1966) Enzyme-labelled antibodies: preparation and application for the localization of antigens. J Histochem Cytochem 14, 929-931
    • (1966) J Histochem Cytochem , vol.14 , pp. 929-931
    • Nakane, P.K.1    Pierce, G.B.2
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK ( 1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 221, 680-685
    • (1970) Nature , vol.221 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 0028075453 scopus 로고
    • EGTA induces the synthesis in Escherichia coli of 3 proteins that cross-react with calmodulin antibodies
    • Laoudj D, Andersen CL, Bras A, Goldberg M, Jacq A, Holland IB (1994) EGTA induces the synthesis in Escherichia coli of 3 proteins that cross-react with calmodulin antibodies. Mol Microbiol 13, 445-457
    • (1994) Mol Microbiol , vol.13 , pp. 445-457
    • Laoudj, D.1    Andersen, C.L.2    Bras, A.3    Goldberg, M.4    Jacq, A.5    Holland, I.B.6
  • 32
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger H, von Jagow G (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa, Anal Biochem 166, 368-379
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 33
    • 0015871909 scopus 로고
    • In vitro synthesis of protein in microbial systems
    • Zubay G (1973) In vitro synthesis of protein in microbial systems. Annu Rev Genet 7, 267-298
    • (1973) Annu Rev Genet , vol.7 , pp. 267-298
    • Zubay, G.1
  • 34
    • 0029055426 scopus 로고
    • A novel activity of OmpT proteolysis under extreme denaturing conditions
    • White CB, Chen Q, Kenyon GL, Babbitt PC (1995) A novel activity of OmpT proteolysis under extreme denaturing conditions J Biol Chem 270, 12990-12994
    • (1995) J Biol Chem , vol.270 , pp. 12990-12994
    • White, C.B.1    Chen, Q.2    Kenyon, G.L.3    Babbitt, P.C.4
  • 35
    • 0028040011 scopus 로고
    • New outer membrane protease of Escherichia coli K-12
    • Kaufmann A, Stierhof Y-D, Henning U (1994) New outer membrane protease of Escherichia coli K-12. J Bacteriol 176, 359-367
    • (1994) J Bacteriol , vol.176 , pp. 359-367
    • Kaufmann, A.1    Stierhof, Y.-D.2    Henning, U.3
  • 36
    • 0028036767 scopus 로고
    • DNA-binding protein H-NS is required for the efficient adaptation of E coli K-12 to a cold environment
    • Dersch P, Kneip S, Bremer E (1994) DNA-binding protein H-NS is required for the efficient adaptation of E coli K-12 to a cold environment. Mol Gen Genet 245, 255-259
    • (1994) Mol Gen Genet , vol.245 , pp. 255-259
    • Dersch, P.1    Kneip, S.2    Bremer, E.3
  • 38
    • 0030601826 scopus 로고    scopus 로고
    • Systematic mutational analysis revealing the functional domain organization of E coli nucleoid protein H-NS
    • Ueguchi C, Suzuki T, Yoshida T, Tanaka K, Mizuno T (1996) Systematic mutational analysis revealing the functional domain organization of E coli nucleoid protein H-NS. J Mol Biol 263, 149-162
    • (1996) J Mol Biol , vol.263 , pp. 149-162
    • Ueguchi, C.1    Suzuki, T.2    Yoshida, T.3    Tanaka, K.4    Mizuno, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.