메뉴 건너뛰기




Volumn 110, Issue 42, 2013, Pages 16814-16819

Discovery of novel chemoeffectors and rational design of Escherichia coli chemoreceptor specificity

Author keywords

[No Author keywords available]

Indexed keywords

CARBONYL DERIVATIVE; CHEMOTACTIC FACTOR; TAR CHEMOTACTIC FACTOR; UNCLASSIFIED DRUG;

EID: 84885807469     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1306811110     Document Type: Article
Times cited : (44)

References (43)
  • 2
    • 0031455398 scopus 로고    scopus 로고
    • The two-component signaling pathway of bacterial chemotaxis: A molecular view of signal transduction by receptors, kinases, and adaptation enzymes
    • Falke JJ, Bass RB, Butler SL, Chervitz SA, Danielson MA (1997) The two-component signaling pathway of bacterial chemotaxis: A molecular view of signal transduction by receptors, kinases, and adaptation enzymes. Annu Rev Cell Dev Biol 13: 457-512.
    • (1997) Annu Rev Cell Dev Biol , vol.13 , pp. 457-512
    • Falke, J.J.1    Bass, R.B.2    Butler, S.L.3    Chervitz, S.A.4    Danielson, M.A.5
  • 3
    • 33645215770 scopus 로고    scopus 로고
    • Signal transduction in bacterial chemotaxis
    • Baker MD, Wolanin PM, Stock JB (2006) Signal transduction in bacterial chemotaxis. Bioessays 28(1): 9-22.
    • (2006) Bioessays , vol.28 , Issue.1 , pp. 9-22
    • Baker, M.D.1    Wolanin, P.M.2    Stock, J.B.3
  • 4
    • 37749029507 scopus 로고    scopus 로고
    • Bacterial chemoreceptors: High-performance signaling in networked arrays
    • Hazelbauer GL, Falke JJ, Parkinson JS (2008) Bacterial chemoreceptors: High-performance signaling in networked arrays. Trends Biochem Sci 33(1): 9-19.
    • (2008) Trends Biochem Sci , vol.33 , Issue.1 , pp. 9-19
    • Hazelbauer, G.L.1    Falke, J.J.2    Parkinson, J.S.3
  • 5
    • 77949917744 scopus 로고    scopus 로고
    • Bacterial chemoreceptors: Providing enhanced features to two-component signaling
    • Hazelbauer GL, Lai WC (2010) Bacterial chemoreceptors: Providing enhanced features to two-component signaling. Curr Opin Microbiol 13(2): 124-132.
    • (2010) Curr Opin Microbiol , vol.13 , Issue.2 , pp. 124-132
    • Hazelbauer, G.L.1    Lai, W.C.2
  • 6
    • 0018712142 scopus 로고
    • Membrane receptors for aspartate and serine in bacterial chemotaxis
    • Clarke S, Koshland DE, Jr. (1979) Membrane receptors for aspartate and serine in bacterial chemotaxis. J Biol Chem 254(19): 9695-9702.
    • (1979) J Biol Chem , vol.254 , Issue.19 , pp. 9695-9702
    • Clarke, S.1    Koshland Jr., D.E.2
  • 7
    • 0020014666 scopus 로고
    • Bacterial chemotaxis
    • Boyd A, Simon M (1982) Bacterial chemotaxis. Annu Rev Physiol 44: 501-517.
    • (1982) Annu Rev Physiol , vol.44 , pp. 501-517
    • Boyd, A.1    Simon, M.2
  • 8
    • 35348842602 scopus 로고    scopus 로고
    • Bacterial sensor kinase TodS interacts with agonistic and antagonistic signals
    • Busch A, Lacal J, Martos A, Ramos JL, Krell T (2007) Bacterial sensor kinase TodS interacts with agonistic and antagonistic signals. Proc Natl Acad Sci USA 104(34): 13774-13779.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.34 , pp. 13774-13779
    • Busch, A.1    Lacal, J.2    Martos, A.3    Ramos, J.L.4    Krell, T.5
  • 9
    • 0031559942 scopus 로고    scopus 로고
    • Apo structure of the ligand-binding domain of aspartate receptor from Escherichia coli and its comparison with ligand-bound or pseudoligand-bound structures
    • Chi YI, Yokota H, Kim SH (1997) Apo structure of the ligand-binding domain of aspartate receptor from Escherichia coli and its comparison with ligand-bound or pseudoligand-bound structures. FEBS Lett 414(2): 327-332.
    • (1997) FEBS Lett , vol.414 , Issue.2 , pp. 327-332
    • Chi, Y.I.1    Yokota, H.2    Kim, S.H.3
  • 10
    • 0026315513 scopus 로고
    • Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand
    • Milburn MV, et al. (1991) Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand. Science 254(5036): 1342-1347.
    • (1991) Science , vol.254 , Issue.5036 , pp. 1342-1347
    • Milburn, M.V.1
  • 11
    • 0027175202 scopus 로고
    • The three-dimensional structure of the ligand-binding domain of a wild-type bacterial chemotaxis receptor. Structural comparison to the cross-linked mutant forms and conformational changes upon ligand binding
    • Yeh JI, Biemann HP, Pandit J, Koshland DE, Jr., Kim SH (1993) The three-dimensional structure of the ligand-binding domain of a wild-type bacterial chemotaxis receptor. Structural comparison to the cross-linked mutant forms and conformational changes upon ligand binding. J Biol Chem 268(13): 9787-9792.
    • (1993) J Biol Chem , vol.268 , Issue.13 , pp. 9787-9792
    • Yeh, J.I.1    Biemann, H.P.2    Pandit, J.3    Koshland Jr., D.E.4    Kim, S.H.5
  • 12
    • 0030595334 scopus 로고    scopus 로고
    • High-resolution structures of the ligand binding domain of the wild-type bacterial aspartate receptor
    • Yeh JI, et al. (1996) High-resolution structures of the ligand binding domain of the wild-type bacterial aspartate receptor. J Mol Biol 262(2): 186-201.
    • (1996) J Mol Biol , vol.262 , Issue.2 , pp. 186-201
    • Yeh, J.I.1
  • 13
    • 0028818765 scopus 로고
    • Lock on/off disulfides identify the transmembrane signaling helix of the aspartate receptor
    • Chervitz SA, Falke JJ (1995) Lock on/off disulfides identify the transmembrane signaling helix of the aspartate receptor. J Biol Chem 270(41): 24043-24053.
    • (1995) J Biol Chem , vol.270 , Issue.41 , pp. 24043-24053
    • Chervitz, S.A.1    Falke, J.J.2
  • 14
    • 0035312774 scopus 로고    scopus 로고
    • Transmembrane signaling in bacterial chemoreceptors
    • Falke JJ, Hazelbauer GL (2001) Transmembrane signaling in bacterial chemoreceptors. Trends Biochem Sci 26(4): 257-265.
    • (2001) Trends Biochem Sci , vol.26 , Issue.4 , pp. 257-265
    • Falke, J.J.1    Hazelbauer, G.L.2
  • 15
    • 0029851704 scopus 로고    scopus 로고
    • Attractant signaling by an aspartate chemoreceptor dimer with a single cytoplasmic domain
    • Gardina PJ, Manson MD (1996) Attractant signaling by an aspartate chemoreceptor dimer with a single cytoplasmic domain. Science 274(5286): 425-426.
    • (1996) Science , vol.274 , Issue.5286 , pp. 425-426
    • Gardina, P.J.1    Manson, M.D.2
  • 16
    • 0029910912 scopus 로고    scopus 로고
    • Detecting the conformational change of transmembrane signaling in a bacterial chemoreceptor by measuring effects on disulfide cross-linking in vivo
    • Hughson AG, Hazelbauer GL (1996) Detecting the conformational change of transmembrane signaling in a bacterial chemoreceptor by measuring effects on disulfide cross-linking in vivo. Proc Natl Acad Sci USA 93(21): 11546-11551.
    • (1996) Proc Natl Acad Sci USA , vol.93 , Issue.21 , pp. 11546-11551
    • Hughson, A.G.1    Hazelbauer, G.L.2
  • 17
    • 0027127956 scopus 로고
    • The fifth datta lecture. Structural similarities between the aspartate receptor of bacterial chemotaxis and the trp repressor of E coli. Implications for transmembrane signaling
    • Lynch BA, Koshland DE, Jr. (1992) The fifth Datta Lecture. Structural similarities between the aspartate receptor of bacterial chemotaxis and the trp repressor of E. coli. Implications for transmembrane signaling. FEBS Lett 307(1): 3-9.
    • (1992) FEBS Lett , vol.307 , Issue.1 , pp. 3-9
    • Lynch, B.A.1    Koshland Jr., D.E.2
  • 18
    • 0035814825 scopus 로고    scopus 로고
    • Site-directed solid-state NMR measurement of a ligand-induced conformational change in the serine bacterial chemoreceptor
    • Murphy OJ, 3rd, Kovacs FA, Sicard EL, Thompson LK (2001) Site-directed solid-state NMR measurement of a ligand-induced conformational change in the serine bacterial chemoreceptor. Biochemistry 40(5): 1358-1366.
    • (2001) Biochemistry , vol.40 , Issue.5 , pp. 1358-1366
    • Murphy III, O.J.1    Kovacs, F.A.2    Sicard, E.L.3    Thompson, L.K.4
  • 19
    • 0033543590 scopus 로고    scopus 로고
    • A piston model for transmembrane signaling of the aspartate receptor
    • Ottemann KM, Xiao W, Shin YK, Koshland DE, Jr. (1999) A piston model for transmembrane signaling of the aspartate receptor. Science 285(5434): 1751-1754.
    • (1999) Science , vol.285 , Issue.5434 , pp. 1751-1754
    • Ottemann, K.M.1    Xiao, W.2    Shin, Y.K.3    Koshland Jr., D.E.4
  • 20
    • 13444283382 scopus 로고    scopus 로고
    • Tryptophan residues flanking the second transmembrane helix (TM2) set the signaling state of the Tar chemoreceptor
    • Draheim RR, Bormans AF, Lai RZ, Manson MD (2005) Tryptophan residues flanking the second transmembrane helix (TM2) set the signaling state of the Tar chemoreceptor. Biochemistry 44(4): 1268-1277.
    • (2005) Biochemistry , vol.44 , Issue.4 , pp. 1268-1277
    • Draheim, R.R.1    Bormans, A.F.2    Lai, R.Z.3    Manson, M.D.4
  • 21
    • 0035951821 scopus 로고    scopus 로고
    • Mutations that affect ligand binding to the Escherichia coli aspartate receptor: Implications for transmembrane signaling
    • Björkman AM, Dunten P, Sandgren MO, Dwarakanath VN, Mowbray SL (2001) Mutations that affect ligand binding to the Escherichia coli aspartate receptor: Implications for transmembrane signaling. J Biol Chem 276(4): 2808-2815.
    • (2001) J Biol Chem , vol.276 , Issue.4 , pp. 2808-2815
    • Björkman, A.M.1    Dunten, P.2    Sandgren, M.O.3    Dwarakanath, V.N.4    Mowbray, S.L.5
  • 22
    • 0025058595 scopus 로고
    • Role of threonine residue 154 in ligand recognition of the Tar chemoreceptor in Escherichia coli
    • Lee L, Imae Y (1990) Role of threonine residue 154 in ligand recognition of the Tar chemoreceptor in Escherichia coli. J Bacteriol 172(1): 377-382.
    • (1990) J Bacteriol , vol.172 , Issue.1 , pp. 377-382
    • Lee, L.1    Imae, Y.2
  • 23
    • 0025150830 scopus 로고
    • Mutations in the aspartate receptor of Escherichia coli which affect aspartate binding
    • Mowbray SL, Koshland DE, Jr. (1990) Mutations in the aspartate receptor of Escherichia coli which affect aspartate binding. J Biol Chem 265(26): 15638-15643.
    • (1990) J Biol Chem , vol.265 , Issue.26 , pp. 15638-15643
    • Mowbray, S.L.1    Koshland Jr., D.E.2
  • 24
    • 0024093975 scopus 로고
    • Aspartate taxis mutants of the Escherichia coli Tar chemoreceptor
    • Wolff C, Parkinson JS (1988) Aspartate taxis mutants of the Escherichia coli Tar chemoreceptor. J Bacteriol 170(10): 4509-4515.
    • (1988) J Bacteriol , vol.170 , Issue.10 , pp. 4509-4515
    • Wolff, C.1    Parkinson, J.S.2
  • 25
    • 0021057460 scopus 로고
    • Chemotactic response of Escherichia coli to chemically synthesized amino acids
    • Hedblom ML, Adler J (1983) Chemotactic response of Escherichia coli to chemically synthesized amino acids. J Bacteriol 155(3): 1463-1466.
    • (1983) J Bacteriol , vol.155 , Issue.3 , pp. 1463-1466
    • Hedblom, M.L.1    Adler, J.2
  • 26
    • 29444451565 scopus 로고    scopus 로고
    • Changing the specificity of a bacterial chemoreceptor
    • Derr P, Boder E, Goulian M (2006) Changing the specificity of a bacterial chemoreceptor. J Mol Biol 355(5): 923-932.
    • (2006) J Mol Biol , vol.355 , Issue.5 , pp. 923-932
    • Derr, P.1    Boder, E.2    Goulian, M.3
  • 27
    • 77958565592 scopus 로고    scopus 로고
    • Binding energy landscape analysis helps to discriminate true hits from high-scoring decoys in virtual screening
    • Wei D, Zheng H, Su N, Deng M, Lai L (2010) Binding energy landscape analysis helps to discriminate true hits from high-scoring decoys in virtual screening. J Chem Inf Model 50(10): 1855-1864.
    • (2010) J Chem Inf Model , vol.50 , Issue.10 , pp. 1855-1864
    • Wei, D.1    Zheng, H.2    Su, N.3    Deng, M.4    Lai, L.5
  • 28
    • 0345293146 scopus 로고    scopus 로고
    • On the value of c: Can low affinity systems be studied by isothermal titration calorimetry?
    • Turnbull WB, Daranas AH (2003) On the value of c: Can low affinity systems be studied by isothermal titration calorimetry? J Am Chem Soc 125(48): 14859-14866.
    • (2003) J Am Chem Soc , vol.125 , Issue.48 , pp. 14859-14866
    • Turnbull, W.B.1    Daranas, A.H.2
  • 29
    • 37549033509 scopus 로고    scopus 로고
    • Isothermal titration calorimetry at very low c
    • Tellinghuisen J (2008) Isothermal titration calorimetry at very low c. Anal Biochem 373(2): 395-397.
    • (2008) Anal Biochem , vol.373 , Issue.2 , pp. 395-397
    • Tellinghuisen, J.1
  • 30
    • 84863238091 scopus 로고    scopus 로고
    • A parallel diffusion-based microfluidic device for bacterial chemotaxis analysis
    • Si G, Yang W, Bi S, Luo C, Ouyang Q (2012) A parallel diffusion-based microfluidic device for bacterial chemotaxis analysis. Lab Chip 12(7): 1389-1394.
    • (2012) Lab Chip , vol.12 , Issue.7 , pp. 1389-1394
    • Si, G.1    Yang, W.2    Bi, S.3    Luo, C.4    Ouyang, Q.5
  • 31
    • 0037039384 scopus 로고    scopus 로고
    • Receptor sensitivity in bacterial chemotaxis
    • Sourjik V, Berg HC (2002) Receptor sensitivity in bacterial chemotaxis. Proc Natl Acad Sci USA 99(1): 123-127.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.1 , pp. 123-127
    • Sourjik, V.1    Berg, H.C.2
  • 32
    • 85058201627 scopus 로고    scopus 로고
    • In vivo measurement by FRET of pathway activity in bacterial chemotaxis
    • Sourjik V, Vaknin A, Shimizu TS, Berg HC (2007) In vivo measurement by FRET of pathway activity in bacterial chemotaxis. Methods Enzymol 423: 365-391.
    • (2007) Methods Enzymol , vol.423 , pp. 365-391
    • Sourjik, V.1    Vaknin, A.2    Shimizu, T.S.3    Berg, H.C.4
  • 33
    • 77958500295 scopus 로고    scopus 로고
    • Differences in signalling by directly and indirectly binding ligands in bacterial chemotaxis
    • Neumann S, Hansen CH, Wingreen NS, Sourjik V (2010) Differences in signalling by directly and indirectly binding ligands in bacterial chemotaxis. EMBO J 29(20): 3484-3495.
    • (2010) EMBO J , vol.29 , Issue.20 , pp. 3484-3495
    • Neumann, S.1    Hansen, C.H.2    Wingreen, N.S.3    Sourjik, V.4
  • 34
    • 1842473065 scopus 로고    scopus 로고
    • Functional interactions between receptors in bacterial chemotaxis
    • Sourjik V, Berg HC (2004) Functional interactions between receptors in bacterial chemotaxis. Nature 428(6981): 437-441.
    • (2004) Nature , vol.428 , Issue.6981 , pp. 437-441
    • Sourjik, V.1    Berg, H.C.2
  • 35
    • 0015413647 scopus 로고
    • Chemotaxis toward amino acids in Escherichia coli
    • Mesibov R, Adler J (1972) Chemotaxis toward amino acids in Escherichia coli. J Bacteriol 112(1): 315-326.
    • (1972) J Bacteriol , vol.112 , Issue.1 , pp. 315-326
    • Mesibov, R.1    Adler, J.2
  • 37
    • 46749095500 scopus 로고    scopus 로고
    • From virtuality to reality - Virtual screening in lead discovery and lead optimization: A medicinal chemistry perspective
    • Rester U (2008) From virtuality to reality - Virtual screening in lead discovery and lead optimization: a medicinal chemistry perspective. Curr Opin Drug Discov Devel 11(4): 559-568.
    • (2008) Curr Opin Drug Discov Devel , vol.11 , Issue.4 , pp. 559-568
    • Rester, U.1
  • 38
    • 67649295270 scopus 로고    scopus 로고
    • Structure-based design of a periplasmic binding protein antagonist that prevents domain closure
    • Borrok MJ, Zhu Y, Forest KT, Kiessling LL (2009) Structure-based design of a periplasmic binding protein antagonist that prevents domain closure. ACS Chem Biol 4(6): 447-456.
    • (2009) ACS Chem Biol , vol.4 , Issue.6 , pp. 447-456
    • Borrok, M.J.1    Zhu, Y.2    Forest, K.T.3    Kiessling, L.L.4
  • 39
    • 0036221572 scopus 로고    scopus 로고
    • The role of motility as a virulence factor in bacteria
    • Josenhans C, Suerbaum S (2002) The role of motility as a virulence factor in bacteria. Int J Med Microbiol 291(8): 605-614.
    • (2002) Int J Med Microbiol , vol.291 , Issue.8 , pp. 605-614
    • Josenhans, C.1    Suerbaum, S.2
  • 40
    • 0033765049 scopus 로고    scopus 로고
    • Chemotaxis in pathogenic spirochetes: Directed movement toward targeting tissues?
    • Lux R, Moter A, Shi W (2000) Chemotaxis in pathogenic spirochetes: Directed movement toward targeting tissues? J Mol Microbiol Biotechnol 2(4): 355-364.
    • (2000) J Mol Microbiol Biotechnol , vol.2 , Issue.4 , pp. 355-364
    • Lux, R.1    Moter, A.2    Shi, W.3
  • 41
    • 0027295668 scopus 로고
    • Ligand binding induces an asymmetrical transmembrane signal through a receptor dimer
    • Yang Y, Park H, Inouye M (1993) Ligand binding induces an asymmetrical transmembrane signal through a receptor dimer. J Mol Biol 232(2): 493-498.
    • (1993) J Mol Biol , vol.232 , Issue.2 , pp. 493-498
    • Yang, Y.1    Park, H.2    Inouye, M.3
  • 42
    • 33947716119 scopus 로고    scopus 로고
    • A semiempirical free energy force field with charge-based desolvation
    • Huey R, Morris GM, Olson AJ, Goodsell DS (2007) A semiempirical free energy force field with charge-based desolvation. J Comput Chem 28(6): 1145-1152.
    • (2007) J Comput Chem , vol.28 , Issue.6 , pp. 1145-1152
    • Huey, R.1    Morris, G.M.2    Olson, A.J.3    Goodsell, D.S.4
  • 43
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald IK, Thornton JM (1994) Satisfying hydrogen bonding potential in proteins. J Mol Biol 238(5): 777-793.
    • (1994) J Mol Biol , vol.238 , Issue.5 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.