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Volumn 43, Issue 2, 2015, Pages 1283-1296

Structural insight into operator dre-sites recognition and effector binding in the GntR/HutC transcription regulator NagR

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL DNA; BACTERIAL PROTEIN; GLUCOSAMINE; GLUCOSAMINE 6-PHOSPHATE; GLUCOSE 6 PHOSPHATE; N ACETYLGLUCOSAMINE; N-ACETYLGLUCOSAMINE 6-PHOSPHATE; PROTEIN BINDING; REPRESSOR PROTEIN;

EID: 84941123432     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gku1374     Document Type: Article
Times cited : (32)

References (45)
  • 1
    • 0033759266 scopus 로고    scopus 로고
    • Regulation of carbon catabolism in Bacillus species
    • Stülke,J. and Hillen,W. (2000) Regulation of carbon catabolism in Bacillus species. Annu. Rev. Microbiol., 54, 849-880.
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 849-880
    • Stülke, J.1    Hillen, W.2
  • 2
    • 47549110972 scopus 로고    scopus 로고
    • Carbon catabolite repression in bacteria: Many ways to make the most out of nutrients
    • Gorke,B. and Stulke,J. (2008) Carbon catabolite repression in bacteria: many ways to make the most out of nutrients. Nat. Rev. Microbiol., 6, 613-624.
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 613-624
    • Gorke, B.1    Stulke, J.2
  • 3
    • 79960386471 scopus 로고    scopus 로고
    • Regulon of the N-Acetylglucosamine Utilization Regulator NagR in Bacillus subtilis
    • Bertram,R., Rigali,S., Wood,N., Lulko,A.T., Kuipers,O.P. and Titgemeyer,F. (2011) Regulon of the N-Acetylglucosamine Utilization Regulator NagR in Bacillus subtilis. J. Bacteriol., 193, 3525-3536.
    • (2011) J. Bacteriol. , vol.193 , pp. 3525-3536
    • Bertram, R.1    Rigali, S.2    Wood, N.3    Lulko, A.T.4    Kuipers, O.P.5    Titgemeyer, F.6
  • 4
    • 0020472708 scopus 로고
    • Transport and incorporation of N-acetyl-D-glucosamine in Bacillus subtilis
    • Mobley,H.L., Doyle,R.J., Streips,U.N. and Langemeier,S.O. (1982) Transport and incorporation of N-acetyl-D-glucosamine in Bacillus subtilis. J. Bacteriol., 150, 8-15.
    • (1982) J. Bacteriol. , vol.150 , pp. 8-15
    • Mobley, H.L.1    Doyle, R.J.2    Streips, U.N.3    Langemeier, S.O.4
  • 5
    • 0014250205 scopus 로고
    • N-acetylglucosamine assimilation in Escherichia coli and its relation to catabolite repression
    • Dobrogosz,W.J. (1968) N-acetylglucosamine assimilation in Escherichia coli and its relation to catabolite repression. J. Bacteriol., 95, 585-591.
    • (1968) J. Bacteriol. , vol.95 , pp. 585-591
    • Dobrogosz, W.J.1
  • 6
    • 46449120734 scopus 로고    scopus 로고
    • Feast or famine: The global regulator DasR links nutrient stress to antibiotic production by Streptomyces
    • Rigali,S., Titgemeyer,F., Barends,S., Mulder,S., Thomae,A.W., Hopwood,D.A. and van Wezel,G.P. (2008) Feast or famine: the global regulator DasR links nutrient stress to antibiotic production by Streptomyces. EMBO Rep., 9, 670-675.
    • (2008) EMBO Rep. , vol.9 , pp. 670-675
    • Rigali, S.1    Titgemeyer, F.2    Barends, S.3    Mulder, S.4    Thomae, A.W.5    Hopwood, D.A.6    Van Wezel, G.P.7
  • 7
    • 77952314977 scopus 로고    scopus 로고
    • Insight into the induction mechanism of the GntR/HutC bacterial transcription regulator YvoA
    • Resch,M., Schiltz,E., Titgemeyer,F. and Muller,Y.A. (2010) Insight into the induction mechanism of the GntR/HutC bacterial transcription regulator YvoA. Nucleic Acids Res., 38, 2485-2497.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 2485-2497
    • Resch, M.1    Schiltz, E.2    Titgemeyer, F.3    Muller, Y.A.4
  • 8
    • 3242674438 scopus 로고    scopus 로고
    • Extending the classification of bacterial transcription factors beyond the helix-turn-helix motif as an alternative approach to discover new cis/trans relationships
    • Rigali,S., Schlicht,M., Hoskisson,P., Nothaft,H., Merzbacher,M., Joris,B. and Titgemeyer,F. (2004) Extending the classification of bacterial transcription factors beyond the helix-turn-helix motif as an alternative approach to discover new cis/trans relationships. Nucleic Acids Res., 32, 3418-3426.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 3418-3426
    • Rigali, S.1    Schlicht, M.2    Hoskisson, P.3    Nothaft, H.4    Merzbacher, M.5    Joris, B.6    Titgemeyer, F.7
  • 9
    • 27644557812 scopus 로고    scopus 로고
    • The two authentic methionine aminopeptidase genes are differentially expressed in Bacillus subtilis
    • You,C., Lu,H., Sekowska,A., Fang,G., Wang,Y., Gilles,A.M. and Danchin,A. (2005) The two authentic methionine aminopeptidase genes are differentially expressed in Bacillus subtilis. BMC Microbiol., 5, 57.
    • (2005) BMC Microbiol. , vol.5 , pp. 57
    • You, C.1    Lu, H.2    Sekowska, A.3    Fang, G.4    Wang, Y.5    Gilles, A.M.6    Danchin, A.7
  • 10
    • 0033376557 scopus 로고    scopus 로고
    • Novel phosphotransferase system genes revealed by genome analysis -The complete complement of PTS proteins encoded within the genome of Bacillus subtilis
    • Reizer,J., Bachem,S., Reizer,A., Arnaud,M., Saier,M.H. Jr and Stülke,J. (1999) Novel phosphotransferase system genes revealed by genome analysis-the complete complement of PTS proteins encoded within the genome of Bacillus subtilis. Microbiology, 145, 3419-3429.
    • (1999) Microbiology , vol.145 , pp. 3419-3429
    • Reizer, J.1    Bachem, S.2    Reizer, A.3    Arnaud, M.4    Saier, M.H.5    Stülke, J.6
  • 11
    • 21244505806 scopus 로고    scopus 로고
    • Structure and kinetics of a monomeric glucosamine 6-phosphate deaminase: Missing link of the NagB superfamily
    • Vincent,F., Davies,G.J. and Brannigan,J.A. (2005) Structure and kinetics of a monomeric glucosamine 6-phosphate deaminase: missing link of the NagB superfamily? J. Biol. Chem., 280, 19649-19655.
    • (2005) J. Biol. Chem. , vol.280 , pp. 19649-19655
    • Vincent, F.1    Davies, G.J.2    Brannigan, J.A.3
  • 12
    • 1642576068 scopus 로고    scopus 로고
    • The three-dimensional structure of the N-acetylglucosamine-6-phosphate deacetylase, NagA, from Bacillus subtilis: A member of the urease superfamily
    • Vincent,F., Yates,D., Garman,E., Davies,G.J. and Brannigan,J.A. (2004) The three-dimensional structure of the N-acetylglucosamine-6-phosphate deacetylase, NagA, from Bacillus subtilis: a member of the urease superfamily. J. Biol. Chem., 279, 2809-2816.
    • (2004) J. Biol. Chem. , vol.279 , pp. 2809-2816
    • Vincent, F.1    Yates, D.2    Garman, E.3    Davies, G.J.4    Brannigan, J.A.5
  • 13
    • 84877258372 scopus 로고    scopus 로고
    • The use of amino sugars by Bacillus subtilis: Presence of a unique operon for the catabolism of glucosamine
    • Gaugue,I., Oberto,J., Putzer,H. and Plumbridge,J. (2013) The use of amino sugars by Bacillus subtilis: presence of a unique operon for the catabolism of glucosamine. PLoS One, 8, e63025.
    • (2013) PLoS One , vol.8 , pp. e63025
    • Gaugue, I.1    Oberto, J.2    Putzer, H.3    Plumbridge, J.4
  • 14
    • 84897110696 scopus 로고    scopus 로고
    • Regulation of amino sugar utilization in Bacillus subtilis by the GntR family regulators, NagR and GamR
    • Gaugue,I., Oberto,J. and Plumbridge,J. (2014) Regulation of amino sugar utilization in Bacillus subtilis by the GntR family regulators, NagR and GamR. Mol. Microbiol., 92, 100-115.
    • (2014) Mol. Microbiol. , vol.92 , pp. 100-115
    • Gaugue, I.1    Oberto, J.2    Plumbridge, J.3
  • 15
    • 33747043508 scopus 로고    scopus 로고
    • The sugar phosphotransferase system of Streptomyces coelicolor is regulated by the GntR-family regulator DasR and links N-acetylglucosamine metabolism to the control of development
    • Rigali,S., Nothaft,H., Noens,E.E., Schlicht,M., Colson,S., Muller,M., Joris,B., Koerten,H.K., Hopwood,D.A., Titgemeyer,F. et al. (2006) The sugar phosphotransferase system of Streptomyces coelicolor is regulated by the GntR-family regulator DasR and links N-acetylglucosamine metabolism to the control of development. Mol. Microbiol., 61, 1237-1251.
    • (2006) Mol. Microbiol. , vol.61 , pp. 1237-1251
    • Rigali, S.1    Nothaft, H.2    Noens, E.E.3    Schlicht, M.4    Colson, S.5    Muller, M.6    Joris, B.7    Koerten, H.K.8    Hopwood, D.A.9    Titgemeyer, F.10
  • 16
    • 0037066712 scopus 로고    scopus 로고
    • Subdivision of the helix-turn-helix GntR family of bacterial regulators in the FadR, HutC, MocR, and YtrA subfamilies
    • Rigali,S., Derouaux,A., Giannotta,F. and Dusart,J. (2002) Subdivision of the helix-turn-helix GntR family of bacterial regulators in the FadR, HutC, MocR, and YtrA subfamilies. J. Biol. Chem., 277, 12507-12515.
    • (2002) J. Biol. Chem. , vol.277 , pp. 12507-12515
    • Rigali, S.1    Derouaux, A.2    Giannotta, F.3    Dusart, J.4
  • 17
    • 69249166013 scopus 로고    scopus 로고
    • Chapter 1: Variation in form and function the helix-turn-helix regulators of the GntR superfamily
    • Hoskisson,P.A. and Rigali,S. (2009) Chapter 1: variation in form and function the helix-turn-helix regulators of the GntR superfamily. Adv. Appl. Microbiol., 69, 1-22.
    • (2009) Adv. Appl. Microbiol. , vol.69 , pp. 1-22
    • Hoskisson, P.A.1    Rigali, S.2
  • 19
    • 0038664315 scopus 로고    scopus 로고
    • HutC/FarR-like bacterial transcription factors of the GntR family contain a small molecule-binding domain of the chorismate lyase fold
    • Aravind,L. and Anantharaman,V. (2003) HutC/FarR-like bacterial transcription factors of the GntR family contain a small molecule-binding domain of the chorismate lyase fold. FEMS Microbiol. Lett., 222, 17-23.
    • (2003) FEMS Microbiol. Lett. , vol.222 , pp. 17-23
    • Aravind, L.1    Anantharaman, V.2
  • 24
    • 84861425552 scopus 로고    scopus 로고
    • Linking crystallographic model and data quality
    • Karplus,P.A. and Diederichs,K. (2012) Linking crystallographic model and data quality. Science, 336, 1030-1033.
    • (2012) Science , vol.336 , pp. 1030-1033
    • Karplus, P.A.1    Diederichs, K.2
  • 25
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy,A.J. (2007) Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr. D Biol. Crystallogr., 63, 32-41.
    • (2007) Acta Crystallogr. D Biol. Crystallogr. , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 30
    • 0031574026 scopus 로고    scopus 로고
    • NUCPLOT: A program to generate schematic diagrams of protein-nucleic acid interactions
    • Luscombe,N.M., Laskowski,R.A. and Thornton,J.M. (1997) NUCPLOT: a program to generate schematic diagrams of protein-nucleic acid interactions. Nucleic Acids Res., 25, 4940-4945.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4940-4945
    • Luscombe, N.M.1    Laskowski, R.A.2    Thornton, J.M.3
  • 31
    • 80054911951 scopus 로고    scopus 로고
    • LigPlot+: Multiple ligand-protein interaction diagrams for drug discovery
    • Laskowski,R.A. and Swindells,M.B. (2011) LigPlot+: multiple ligand-protein interaction diagrams for drug discovery. J. Chem. Inf. Model., 51, 2778-2786.
    • (2011) J. Chem. Inf. Model. , vol.51 , pp. 2778-2786
    • Laskowski, R.A.1    Swindells, M.B.2
  • 32
    • 84893482610 scopus 로고
    • A solution for the best rotation to relate two sets of vectors
    • Kabsch,W. (1976) A solution for the best rotation to relate two sets of vectors. Acta Crystallogr. A, 32, 922-923.
    • (1976) Acta Crystallogr. A , vol.32 , pp. 922-923
    • Kabsch, W.1
  • 35
    • 0021978310 scopus 로고
    • The role of the alpha-helix dipole in protein function and structure
    • Hol,W.G. (1985) The role of the alpha-helix dipole in protein function and structure. Prog. Biophys. Mol. Biol., 45, 149-195.
    • (1985) Prog. Biophys. Mol. Biol. , vol.45 , pp. 149-195
    • Hol, W.G.1
  • 36
    • 0019837215 scopus 로고
    • Nature of the charge distribution in proteins
    • Wada,A. and Nakamura,H. (1981) Nature of the charge distribution in proteins. Nature, 293, 757-758.
    • (1981) Nature , vol.293 , pp. 757-758
    • Wada, A.1    Nakamura, H.2
  • 37
    • 4444261821 scopus 로고    scopus 로고
    • Role of CH/pi interactions in substrate binding by Escherichia coli beta-galactosidase
    • Spiwok,V., Lipovova,P., Skalova,T., Buchtelova,E., Hasek,J. and Kralova,B. (2004) Role of CH/pi interactions in substrate binding by Escherichia coli beta-galactosidase. Carbohydr. Res., 339, 2275-2280.
    • (2004) Carbohydr. Res. , vol.339 , pp. 2275-2280
    • Spiwok, V.1    Lipovova, P.2    Skalova, T.3    Buchtelova, E.4    Hasek, J.5    Kralova, B.6
  • 38
    • 0242417008 scopus 로고    scopus 로고
    • Interactions with aromatic rings in chemical and biological recognition
    • Meyer,E.A., Castellano,R.K. and Diederich,F. (2003) Interactions with aromatic rings in chemical and biological recognition. Angew. Chem. Int. Ed. Engl., 42, 1210-1250.
    • (2003) Angew. Chem. Int. Ed. Engl. , vol.42 , pp. 1210-1250
    • Meyer, E.A.1    Castellano, R.K.2    Diederich, F.3
  • 39
    • 84871771101 scopus 로고    scopus 로고
    • Spacing between core recognition motifs determines relative orientation of AraR monomers on bipartite operators
    • Jain,D. and Nair,D.T. (2013) Spacing between core recognition motifs determines relative orientation of AraR monomers on bipartite operators. Nucleic Acids Res., 41, 639-647.
    • (2013) Nucleic Acids Res. , vol.41 , pp. 639-647
    • Jain, D.1    Nair, D.T.2
  • 41
    • 0036468362 scopus 로고    scopus 로고
    • Prokaryotic transcription regulators: More than just the helix-turn-helix motif
    • Huffman,J.L. and Brennan,R.G. (2002) Prokaryotic transcription regulators: more than just the helix-turn-helix motif. Curr. Opin. Struct. Biol., 12, 98-106.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 98-106
    • Huffman, J.L.1    Brennan, R.G.2
  • 42
    • 0028566270 scopus 로고
    • A revised set of potentials for beta-turn formation in proteins
    • Hutchinson,E.G. and Thornton,J.M. (1994) A revised set of potentials for beta-turn formation in proteins. Protein Sci., 3, 2207-2216.
    • (1994) Protein Sci. , vol.3 , pp. 2207-2216
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 43
    • 0035907285 scopus 로고    scopus 로고
    • The FadR DNA complex. Transcriptional control of fatty acid metabolism in Escherichia coli
    • Xu,Y., Heath,R.J., Li,Z., Rock,C.O. and White,S.W. (2001) The FadR.DNA complex. Transcriptional control of fatty acid metabolism in Escherichia coli. J. Biol. Chem., 276, 17373-17379.
    • (2001) J. Biol. Chem. , vol.276 , pp. 17373-17379
    • Xu, Y.1    Heath, R.J.2    Li, Z.3    Rock, C.O.4    White, S.W.5
  • 44
    • 0035901537 scopus 로고    scopus 로고
    • The structural basis of acyl coenzyme A-dependent regulation of the transcription factor FadR
    • van Aalten,D.M., DiRusso,C.C. and Knudsen,J. (2001) The structural basis of acyl coenzyme A-dependent regulation of the transcription factor FadR. EMBO J., 20, 2041-2050.
    • (2001) EMBO J. , vol.20 , pp. 2041-2050
    • Van Aalten, D.M.1    DiRusso, C.C.2    Knudsen, J.3


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