메뉴 건너뛰기




Volumn 15, Issue 5, 2004, Pages 677-687

Salmonella typhimurium recognizes a chemically distinct form of the bacterial quorum-sensing signal AI-2

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLACETONE; BACTERIAL PROTEIN; BINDING PROTEIN; PROTEIN LSRB; TETRAHYDROFURAN DERIVATIVE; UNCLASSIFIED DRUG;

EID: 4444332516     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2004.07.020     Document Type: Article
Times cited : (459)

References (38)
  • 1
    • 0037123780 scopus 로고    scopus 로고
    • Small talk: Cell-to-cell communication in bacteria
    • Bassler B.L. Small talk. cell-to-cell communication in bacteria Cell. 109:2002;421-424
    • (2002) Cell , vol.109 , pp. 421-424
    • Bassler, B.L.1
  • 2
    • 0028228175 scopus 로고
    • Multiple signalling systems controlling expression of luminescence in Vibrio harveyi: Sequence and function of genes encoding a second sensory pathway
    • Bassler B.L., Wright M., Silverman M.R. Multiple signalling systems controlling expression of luminescence in Vibrio harveyi. sequence and function of genes encoding a second sensory pathway Mol. Microbiol. 13:1994;273-286
    • (1994) Mol. Microbiol. , vol.13 , pp. 273-286
    • Bassler, B.L.1    Wright, M.2    Silverman, M.R.3
  • 3
    • 0030911799 scopus 로고    scopus 로고
    • Cross-species induction of luminescence in the quorum-sensing bacterium Vibrio harveyi
    • Bassler B.L., Greenberg E.P., Stevens A.M. Cross-species induction of luminescence in the quorum-sensing bacterium Vibrio harveyi. J. Bacteriol. 179:1997;4043-4045
    • (1997) J. Bacteriol. , vol.179 , pp. 4043-4045
    • Bassler, B.L.1    Greenberg, E.P.2    Stevens, A.M.3
  • 4
    • 0027247722 scopus 로고
    • Intercellular signalling in Vibrio harveyi: Sequence and function of genes regulating expression of luminescence
    • Bassler B.L., Wright M., Showalter R.E., Silverman M.R. Intercellular signalling in Vibrio harveyi. sequence and function of genes regulating expression of luminescence Mol. Microbiol. 9:1993;773-786
    • (1993) Mol. Microbiol. , vol.9 , pp. 773-786
    • Bassler, B.L.1    Wright, M.2    Showalter, R.E.3    Silverman, M.R.4
  • 5
    • 0032698266 scopus 로고    scopus 로고
    • Boron stimulates yeast (Saccharomyces cerevisiae) growth
    • Bennett A., Rowe R.I., Soch N., Eckhert C.D. Boron stimulates yeast (Saccharomyces cerevisiae) growth. J. Nutr. 129:1999;2236-2238
    • (1999) J. Nutr. , vol.129 , pp. 2236-2238
    • Bennett, A.1    Rowe, R.I.2    Soch, N.3    Eckhert, C.D.4
  • 6
    • 0032511137 scopus 로고    scopus 로고
    • Multiple open forms of ribose-binding protein trace the path of its conformational change
    • Bjorkman A.J., Mowbray S.L. Multiple open forms of ribose-binding protein trace the path of its conformational change. J. Mol. Biol. 279:1998;651-664
    • (1998) J. Mol. Biol. , vol.279 , pp. 651-664
    • Bjorkman, A.J.1    Mowbray, S.L.2
  • 9
    • 0028103275 scopus 로고
    • The (Collaborative Computational Project Number 4) CCP4 suite: Programs for protein crystallography
    • CCP4 The (Collaborative Computational Project Number 4) CCP4 suite. programs for protein crystallography Acta Crystallogr. D Biol. Crystallogr. 50:1994;760-763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 10
    • 0032481609 scopus 로고    scopus 로고
    • Cloning and expression of Escherichia coli 5′-methylthioadenosine/ S-adenosylhomocysteine nucleosidase: Identification of the pfs gene product
    • Cornell K.A., Riscoe M.K. Cloning and expression of Escherichia coli 5′-methylthioadenosine/S-adenosylhomocysteine nucleosidase. identification of the pfs gene product Biochim. Biophys. Acta. 1396:1998;8-14
    • (1998) Biochim. Biophys. Acta , vol.1396 , pp. 8-14
    • Cornell, K.A.1    Riscoe, M.K.2
  • 12
    • 0031045585 scopus 로고    scopus 로고
    • Preparation of selenomethionyl proteins for phase determination
    • Doublié S. Preparation of selenomethionyl proteins for phase determination. Methods Enzymol. 276:1997;523-530
    • (1997) Methods Enzymol. , vol.276 , pp. 523-530
    • Doublié, S.1
  • 13
    • 0032927738 scopus 로고    scopus 로고
    • A genetic analysis of the function of LuxO, a two-component response regulator involved in quorum sensing in Vibrio harveyi
    • Freeman J.A., Bassler B.L. A genetic analysis of the function of LuxO, a two-component response regulator involved in quorum sensing in Vibrio harveyi. Mol. Microbiol. 31:1999;665-677
    • (1999) Mol. Microbiol. , vol.31 , pp. 665-677
    • Freeman, J.A.1    Bassler, B.L.2
  • 14
    • 0018424632 scopus 로고
    • Induction of luciferase synthesis in Beneckea harveyi by other marine bacteria
    • Greenberg E.P., Hastings J.W., Ulitzer S. Induction of luciferase synthesis in Beneckea harveyi by other marine bacteria. Arch. Microbiol. 120:1979;87-91
    • (1979) Arch. Microbiol. , vol.120 , pp. 87-91
    • Greenberg, E.P.1    Hastings, J.W.2    Ulitzer, S.3
  • 15
    • 0031677841 scopus 로고    scopus 로고
    • Crystal structure of the effector-binding domain of the trehalose-repressor of Escherichia coli, a member of the LacI family, in its complexes with inducer trehalose-6-phosphate and noninducer trehalose
    • Hars U., Horlacher R., Boos W., Welte W., Diederichs K. Crystal structure of the effector-binding domain of the trehalose-repressor of Escherichia coli, a member of the LacI family, in its complexes with inducer trehalose-6-phosphate and noninducer trehalose. Protein Sci. 7:1998;2511-2521
    • (1998) Protein Sci. , vol.7 , pp. 2511-2521
    • Hars, U.1    Horlacher, R.2    Boos, W.3    Welte, W.4    Diederichs, K.5
  • 16
    • 0036888353 scopus 로고    scopus 로고
    • Improvements in the analysis of domain motions in proteins from conformational change: DynDom version 1.50
    • Hayward S., Lee R.A. Improvements in the analysis of domain motions in proteins from conformational change. DynDom version 1.50 J. Mol. Graph. Model. 21:2002;181-183
    • (2002) J. Mol. Graph. Model. , vol.21 , pp. 181-183
    • Hayward, S.1    Lee, R.A.2
  • 17
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.-Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47:1991;110-119
    • (1991) Acta Crystallogr. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 21
    • 0026509355 scopus 로고
    • Chemistry and biology of boron
    • Loomis W.D., Durst R.W. Chemistry and biology of boron. Biofactors. 3:1992;229-239
    • (1992) Biofactors , vol.3 , pp. 229-239
    • Loomis, W.D.1    Durst, R.W.2
  • 24
    • 0027112289 scopus 로고
    • 1.7 Å X-ray structure of the periplasmic ribose receptor from Escherichia coli
    • Mowbray S.L., Cole L.B. 1.7 Å X-ray structure of the periplasmic ribose receptor from Escherichia coli. J. Mol. Biol. 225:1992;155-175
    • (1992) J. Mol. Biol. , vol.225 , pp. 155-175
    • Mowbray, S.L.1    Cole, L.B.2
  • 25
    • 0021099702 scopus 로고
    • The x-ray structure of the periplasmic galactose binding protein from Salmonella typhimurium at 3.0-Å resolution
    • Mowbray S.L., Petsko G.A. The x-ray structure of the periplasmic galactose binding protein from Salmonella typhimurium at 3.0-Å resolution. J. Biol. Chem. 258:1983;7991-7997
    • (1983) J. Biol. Chem. , vol.258 , pp. 7991-7997
    • Mowbray, S.L.1    Petsko, G.A.2
  • 26
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1998;307-326
    • (1998) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 27
    • 0034897764 scopus 로고    scopus 로고
    • The LuxS family of bacterial autoinducers: Biosynthesis of a novel quorum sensing signal molecule
    • Schauder S., Shokat K., Surette M.G., Bassler B.L. The LuxS family of bacterial autoinducers. biosynthesis of a novel quorum sensing signal molecule Mol. Microbiol. 41:2001;463-476
    • (2001) Mol. Microbiol. , vol.41 , pp. 463-476
    • Schauder, S.1    Shokat, K.2    Surette, M.G.3    Bassler, B.L.4
  • 28
    • 0028173030 scopus 로고
    • Crystal structure of LacI member, PurR, bound to DNA: Minor groove binding by alpha helices
    • Schumacher M.A., Choi K.Y., Zalkin H., Brennan R.G. Crystal structure of LacI member, PurR, bound to DNA. minor groove binding by alpha helices Science. 266:1994;763-770
    • (1994) Science , vol.266 , pp. 763-770
    • Schumacher, M.A.1    Choi, K.Y.2    Zalkin, H.3    Brennan, R.G.4
  • 29
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • Shindyalov I.N., Bourne P.E. Protein structure alignment by incremental combinatorial extension (CE) of the optimal path. Protein Eng. 11:1998;739-747
    • (1998) Protein Eng. , vol.11 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 30
    • 0033574064 scopus 로고    scopus 로고
    • Quorum sensing in Escherichia coli, Salmonella typhimurium, and Vibrio harveyi: A new family of genes responsible for autoinducer production
    • Surette M.G., Miller M.B., Bassler B.L. Quorum sensing in Escherichia coli, Salmonella typhimurium, and Vibrio harveyi. a new family of genes responsible for autoinducer production Proc. Natl. Acad. Sci. USA. 96:1999;1639-1644
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1639-1644
    • Surette, M.G.1    Miller, M.B.2    Bassler, B.L.3
  • 32
    • 0344826554 scopus 로고    scopus 로고
    • Lsr-mediated transport and processing of AI-2 in Salmonella typhimurium
    • Taga M.E., Miller S.T., Bassler B.L. Lsr-mediated transport and processing of AI-2 in Salmonella typhimurium. Mol. Microbiol. 50:2003;1411-1427
    • (2003) Mol. Microbiol. , vol.50 , pp. 1411-1427
    • Taga, M.E.1    Miller, S.T.2    Bassler, B.L.3
  • 33
    • 0035171969 scopus 로고    scopus 로고
    • The LuxS-dependent autoinducer AI-2 controls the expression of an ABC transporter that functions in AI-2 uptake in Salmonella typhimurium
    • Taga M.E., Semmelhack J.L., Bassler B.L. The LuxS-dependent autoinducer AI-2 controls the expression of an ABC transporter that functions in AI-2 uptake in Salmonella typhimurium. Mol. Microbiol. 42:2001;777-793
    • (2001) Mol. Microbiol. , vol.42 , pp. 777-793
    • Taga, M.E.1    Semmelhack, J.L.2    Bassler, B.L.3
  • 34
    • 0036848846 scopus 로고    scopus 로고
    • Automated structure solution, density modification and model building
    • Terwilliger T.C. Automated structure solution, density modification and model building. Acta Crystallogr. D Biol. Crystallogr. 58:2002;1937-1940
    • (2002) Acta Crystallogr. D Biol. Crystallogr. , vol.58 , pp. 1937-1940
    • Terwilliger, T.C.1
  • 37
    • 0037676088 scopus 로고    scopus 로고
    • LuxS quorum sensing: More than just a numbers game
    • Xavier K.B., Bassler B.L. LuxS quorum sensing. more than just a numbers game Curr. Opin. Microbiol. 6:2003;191-197
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 191-197
    • Xavier, K.B.1    Bassler, B.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.