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Volumn 38, Issue 21, 2010, Pages 7778-7790

Crystal structure of the P2 C-repressor: A binder of non-palindromic direct DNA repeats

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; PALINDROMIC DNA; PROTEIN C;

EID: 78649840375     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkq626     Document Type: Article
Times cited : (8)

References (45)
  • 1
    • 23844445773 scopus 로고    scopus 로고
    • Structure of lambda CII: Implications for recognition of direct-repeat DNA by an unusual tetrameric organization
    • Datta, A. B., Panjikar, S., Weiss, M. S., Chakrabarti, P. and Parrack, P. (2005) Structure of lambda CII: implications for recognition of direct-repeat DNA by an unusual tetrameric organization. Proc. Natl Acad. Sci. USA, 102, 11242-11247.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 11242-11247
    • Datta, A.B.1    Panjikar, S.2    Weiss, M.S.3    Chakrabarti, P.4    Parrack, P.5
  • 3
    • 33645528243 scopus 로고    scopus 로고
    • Structures of omega repressors bound to direct and inverted DNA repeats explain modulation of transcription
    • Weihofen, W. A., Cicek, A., Pratto, F., Alonso, J. C. and Saenger, W. (2006) Structures of omega repressors bound to direct and inverted DNA repeats explain modulation of transcription. Nucleic Acids Res., 34, 1450-1458.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 1450-1458
    • Weihofen, W.A.1    Cicek, A.2    Pratto, F.3    Alonso, J.C.4    Saenger, W.5
  • 4
    • 33744730028 scopus 로고    scopus 로고
    • Evolution of immunity and host chromosome integration site of P2-like coliphages
    • Karlsson, J. L., Cardoso-Palacios, C., Nilsson, A. S. and Haggard-Ljungquist, E. (2006) Evolution of immunity and host chromosome integration site of P2-like coliphages. J. Bacteriol., 188, 3923-3935.
    • (2006) J. Bacteriol. , vol.188 , pp. 3923-3935
    • Karlsson, J.L.1    Cardoso-Palacios, C.2    Nilsson, A.S.3    Haggard-Ljungquist, E.4
  • 5
    • 0021219996 scopus 로고
    • DNA sequences of the repressor gene and operator region of bacteriophage P2
    • Ljungquist, E., Kockum, K. and Bertani, L. E. (1984) DNA sequences of the repressor gene and operator region of bacteriophage P2. Proc. Natl Acad. Sci. USA, 81, 3988-3992.
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 3988-3992
    • Ljungquist, E.1    Kockum, K.2    Bertani, L.E.3
  • 7
    • 0344671598 scopus 로고    scopus 로고
    • The transcriptional switch of bacteriophage WPhi, a P2-related but heteroimmune coliphage
    • Liu, T. and Haggard-Ljungquist, E. (1999) The transcriptional switch of bacteriophage WPhi, a P2-related but heteroimmune coliphage. J. Virol., 73, 9816-9826.
    • (1999) J. Virol. , vol.73 , pp. 9816-9826
    • Liu, T.1    Haggard-Ljungquist, E.2
  • 8
    • 34250843747 scopus 로고    scopus 로고
    • A comparison of the DNA binding and bending capacities and the oligomeric states of the immunity repressors of heteroimmune coliphages P2 and WPhi
    • Ahlgren-Berg, A., Henriksson-Peltola, P., Sehlen, W. and Haggard-Ljungquist, E. (2007) A comparison of the DNA binding and bending capacities and the oligomeric states of the immunity repressors of heteroimmune coliphages P2 and WPhi. Nucleic Acids Res., 35, 3167-3180.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 3167-3180
    • Ahlgren-Berg, A.1    Henriksson-Peltola, P.2    Sehlen, W.3    Haggard-Ljungquist, E.4
  • 9
    • 0031793966 scopus 로고    scopus 로고
    • The e protein of satellite phage P4 acts as an anti-repressor by binding to the C protein of helper phage P2
    • Liu, T., Renberg, S. K. and Haggard-Ljungquist, E. (1998) The E protein of satellite phage P4 acts as an anti-repressor by binding to the C protein of helper phage P2. Mol. Microbiol., 30, 1041-1050.
    • (1998) Mol. Microbiol. , vol.30 , pp. 1041-1050
    • Liu, T.1    Renberg, S.K.2    Haggard-Ljungquist, E.3
  • 13
    • 0013797789 scopus 로고
    • Growth abnormalities in Hfr derivatives of Escherichia coli strain C
    • Sasaki, I. and Bertani, G. (1965) Growth abnormalities in Hfr derivatives of Escherichia coli strain C. Virology, 40, 365-376.
    • (1965) Virology , vol.40 , pp. 365-376
    • Sasaki, I.1    Bertani, G.2
  • 14
    • 0014328132 scopus 로고
    • Abortive induction of bacteriophage P2
    • Bertani, L. E. (1968) Abortive induction of bacteriophage P2. Virology, 36, 87-103.
    • (1968) Virology , vol.36 , pp. 87-103
    • Bertani, L.E.1
  • 16
    • 0030962175 scopus 로고    scopus 로고
    • Derepression of prophage P2 by satellite phage P4: Cloning of the P4 epsilon gene and identification of its product
    • Liu, T., Renberg, S. K. and Haggard-Ljungquist, E. (1997) Derepression of prophage P2 by satellite phage P4: cloning of the P4 epsilon gene and identification of its product. J. Virol., 71, 4502-4508.
    • (1997) J. Virol. , vol.71 , pp. 4502-4508
    • Liu, T.1    Renberg, S.K.2    Haggard-Ljungquist, E.3
  • 17
    • 0023300802 scopus 로고
    • Autoregulation of bacteriophage P2 repressor
    • Saha, S., Lundqvist, B. and Haggard-Ljungquist, E. (1987) Autoregulation of bacteriophage P2 repressor. EMBO J., 6, 809-814.
    • (1987) EMBO J. , vol.6 , pp. 809-814
    • Saha, S.1    Lundqvist, B.2    Haggard-Ljungquist, E.3
  • 18
    • 0021271212 scopus 로고
    • Plasmid vectors for the selection of promoters
    • Brosius, J. (1984) Plasmid vectors for the selection of promoters. Gene, 27, 151-160.
    • (1984) Gene , vol.27 , pp. 151-160
    • Brosius, J.1
  • 19
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 20
    • 0020435972 scopus 로고
    • Recombinant genomes which express chloramphenicol acetyltransferase in mammalian cells
    • Gorman, C. M., Moffat, L. F. and Howard, B. H. (1982) Recombinant genomes which express chloramphenicol acetyltransferase in mammalian cells. Mol. Cell Biol., 2, 1044-1051.
    • (1982) Mol. Cell Biol. , vol.2 , pp. 1044-1051
    • Gorman, C.M.1    Moffat, L.F.2    Howard, B.H.3
  • 21
    • 84873799110 scopus 로고
    • Studies on lysogenesis I. The mode of phage liberation by lysogenic Escherichia coli
    • Bertani, G. (1951) Studies on lysogenesis I. The mode of phage liberation by lysogenic Escherichia coli. J. Bacteriol., 62, 293-300.
    • (1951) J. Bacteriol. , vol.62 , pp. 293-300
    • Bertani, G.1
  • 23
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4. (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D. Biol. Crystallogr., 50, 760-763.
    • (1994) Acta Crystallogr. D. Biol. Crystallogr. , vol.50 , pp. 760-763
  • 26
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin, A. and Teplyakov, A. (1997) MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr., 30, 1022-1025.
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 27
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis, A., Morris, R. and Lamzin, V. S. (1999) Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol., 6, 458-463.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 30
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn, M. D., Isupov, M. N. and Murshudov, G. N. (2001) Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta. Crystallogr. D. Biol. Crystallogr., 57, 122-133.
    • (2001) Acta. Crystallogr. D. Biol. Crystallogr. , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 31
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel, E. and Henrick, K. (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta. Crystallogr. D., 60, 2256-2268.
    • (2004) Acta. Crystallogr. D. , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 32
    • 15944379232 scopus 로고    scopus 로고
    • The many faces of the helix-turn-helix domain: Transcription regulation and beyond
    • Aravind, L., Anantharaman, V., Balaji, S., Babu, M. M. and Iyer, L. M. (2005) The many faces of the helix-turn-helix domain: transcription regulation and beyond. FEMS Microbiol. Rev., 29, 231-262.
    • (2005) FEMS Microbiol. Rev. , vol.29 , pp. 231-262
    • Aravind, L.1    Anantharaman, V.2    Balaji, S.3    Babu, M.M.4    Iyer, L.M.5
  • 33
    • 0024284650 scopus 로고
    • Recognition of a DNA operator by the repressor of phage 434: A view at high resolution
    • Aggarwal, A. K., Rodgers, D. W., Drottar, M., Ptashne, M. and Harrison, S. C. (1988) Recognition of a DNA operator by the repressor of phage 434: a view at high resolution. Science, 242, 899-907.
    • (1988) Science , vol.242 , pp. 899-907
    • Aggarwal, A.K.1    Rodgers, D.W.2    Drottar, M.3    Ptashne, M.4    Harrison, S.C.5
  • 34
    • 49249132732 scopus 로고    scopus 로고
    • Structural analysis of the genetic switch that regulates the expression of restriction-modification genes
    • McGeehan, J. E., Streeter, S. D., Thresh, S. J., Ball, N., Ravelli, R. B. and Kneale, G. G. (2008) Structural analysis of the genetic switch that regulates the expression of restriction-modification genes. Nucleic Acids Res., 36, 4778-4787.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 4778-4787
    • McGeehan, J.E.1    Streeter, S.D.2    Thresh, S.J.3    Ball, N.4    Ravelli, R.B.5    Kneale, G.G.6
  • 35
    • 39749145842 scopus 로고    scopus 로고
    • P22 c2 Repressor-Operator Complex: Mechanisms of Direct and Indirect Readout
    • Watkins, D., Hsiao, C., Woods, K. K., Koudelka, G. B. and Williams, L. D. (2008) P22 c2 Repressor-Operator Complex: Mechanisms of Direct and Indirect Readout. Biochemistry, 47, 2325-2338.
    • (2008) Biochemistry , vol.47 , pp. 2325-2338
    • Watkins, D.1    Hsiao, C.2    Woods, K.K.3    Koudelka, G.B.4    Williams, L.D.5
  • 36
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E. and Henrick, K. (2007) Inference of macromolecular assemblies from crystalline state. J. Mol. Biol., 372, 774-797.
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 37
    • 0034034250 scopus 로고    scopus 로고
    • Interacting interfaces of the P4 antirepressor e and the P2 immunity repressor C
    • Eriksson, S. K., Liu, T. and Haggard-Ljungquist, E. (2000) Interacting interfaces of the P4 antirepressor E and the P2 immunity repressor C. Mol. Microbiol., 36, 1148-1155.
    • (2000) Mol. Microbiol. , vol.36 , pp. 1148-1155
    • Eriksson, S.K.1    Liu, T.2    Haggard-Ljungquist, E.3
  • 38
    • 0036500260 scopus 로고    scopus 로고
    • Structural basis for cooperative DNA binding by two dimers of the multidrug-binding protein QacR
    • Schumacher, M. A., Miller, M. C., Grkovic, S., Brown, M. H., Skurray, R. A. and Brennan, R. G. (2002) Structural basis for cooperative DNA binding by two dimers of the multidrug-binding protein QacR. EMBO J., 21, 1210-1218.
    • (2002) EMBO J. , vol.21 , pp. 1210-1218
    • Schumacher, M.A.1    Miller, M.C.2    Grkovic, S.3    Brown, M.H.4    Skurray, R.A.5    Brennan, R.G.6
  • 39
    • 0038713237 scopus 로고    scopus 로고
    • A unified model for the origin of DNA sequence-directed curvature
    • Hud, N. V. and Plavec, J. (2003) A unified model for the origin of DNA sequence-directed curvature. Biopolymers, 69, 144-158.
    • (2003) Biopolymers , vol.69 , pp. 144-158
    • Hud, N.V.1    Plavec, J.2
  • 40
    • 0035393302 scopus 로고    scopus 로고
    • Amino acid-base interactions: A three-dimensional analysis of protein-DNA interactions at an atomic level
    • Luscombe, N. M., Laskowski, R. A. and Thornton, J. M. (2001) Amino acid-base interactions: a three-dimensional analysis of protein-DNA interactions at an atomic level. Nucleic Acids Res., 29, 2860-2874.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2860-2874
    • Luscombe, N.M.1    Laskowski, R.A.2    Thornton, J.M.3
  • 41
    • 0021076118 scopus 로고
    • P22 c2 repressor. Domain structure and function
    • De Anda, J., Poteete, A. R. and Sauer, R. T. (1983) P22 c2 repressor. Domain structure and function. J. Biol. Chem., 258, 10536-10542.
    • (1983) J. Biol. Chem. , vol.258 , pp. 10536-10542
    • De Anda, J.1    Poteete, A.R.2    Sauer, R.T.3
  • 42
    • 0027918646 scopus 로고
    • The complex between phage 434 repressor DNA-binding domain and operator site OR3: Structural differences between consensus and non-consensus half-sites
    • Rodgers, D. W. and Harrison, S. C. (1993) The complex between phage 434 repressor DNA-binding domain and operator site OR3: structural differences between consensus and non-consensus half-sites. Structure, 1, 227-240.
    • (1993) Structure , vol.1 , pp. 227-240
    • Rodgers, D.W.1    Harrison, S.C.2
  • 43
    • 0032584223 scopus 로고    scopus 로고
    • How Cro and lambda-repressor distinguish between operators: The structural basis underlying a genetic switch
    • Albright, R. A. and Matthews, B. W. (1998) How Cro and lambda-repressor distinguish between operators: the structural basis underlying a genetic switch. Proc. Natl Acad. Sci. USA, 95, 3431-3436.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 3431-3436
    • Albright, R.A.1    Matthews, B.W.2
  • 44
    • 0023256884 scopus 로고
    • The crystal structure of trp aporepressor at 1. 8A shows how binding tryptophan enhances DNA affinity
    • Zhang, R. G., Joachimiak, A., Lawson, C. L., Schevitz, R. W., Otwinowski, Z. and Sigler, P. B. (1987) The crystal structure of trp aporepressor at 1. 8A shows how binding tryptophan enhances DNA affinity. Nature, 327, 591-597.
    • (1987) Nature , vol.327 , pp. 591-597
    • Zhang, R.G.1    Joachimiak, A.2    Lawson, C.L.3    Schevitz, R.W.4    Otwinowski, Z.5    Sigler, P.B.6
  • 45
    • 49749208607 scopus 로고
    • Host-dependent induction of phage mutants and lysogenization
    • Bertani, L. E. (1960) Host-dependent induction of phage mutants and lysogenization. Virology, 12, 553-569.
    • (1960) Virology , vol.12 , pp. 553-569
    • Bertani, L.E.1


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