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Volumn 71, Issue 3, 2009, Pages 659-677

The histidine kinase inhibitor Sda binds near the site of autophosphorylation and may sterically hinder autophosphorylation and phosphotransfer to Spo0F

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL ENZYME; ENZYME INHIBITOR; PHOSPHORUS 32; PROTEIN HISTIDINE KINASE; PROTEIN HISTIDINE KINASE KINA; UNCLASSIFIED DRUG;

EID: 58449094352     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2008.06554.x     Document Type: Article
Times cited : (39)

References (46)
  • 1
    • 0036073440 scopus 로고    scopus 로고
    • Inhibition of branched-chain alpha-keto acid dehydrogenase kinase and Sln1 yeast histidine kinase by the antifungal antibiotic radicicol
    • Besant, P.G., Lasker, M.V., Bui, C.D. Turck, C.W. (2002) Inhibition of branched-chain alpha-keto acid dehydrogenase kinase and Sln1 yeast histidine kinase by the antifungal antibiotic radicicol. Mol Pharmacol 62 : 289 296.
    • (2002) Mol Pharmacol , vol.62 , pp. 289-296
    • Besant, P.G.1    Lasker, M.V.2    Bui, C.D.3    Turck, C.W.4
  • 2
    • 0141941680 scopus 로고    scopus 로고
    • Making informed decisions: Regulatory interactions between two-component systems
    • Bijlsma, J.J.E. Groisman, E.A. (2003) Making informed decisions: regulatory interactions between two-component systems. Trends Microbiol 11 : 359 366.
    • (2003) Trends Microbiol , vol.11 , pp. 359-366
    • Bijlsma, J.J.E.1    Groisman, E.A.2
  • 3
    • 0025964291 scopus 로고
    • Initiation of sporulation in B. subtilis is controlled by a multicomponent phosphorelay
    • Burbulys, D., Trach, K.A. Hoch, J.A. (1991) Initiation of sporulation in B. subtilis is controlled by a multicomponent phosphorelay. Cell 64 : 545 552.
    • (1991) Cell , vol.64 , pp. 545-552
    • Burbulys, D.1    Trach, K.A.2    Hoch, J.A.3
  • 4
    • 0035951415 scopus 로고    scopus 로고
    • Replication initiation proteins regulate a developmental checkpoint in Bacillus subtilis
    • Burkholder, W.F., Kurtser, I. Grossman, A.D. (2001) Replication initiation proteins regulate a developmental checkpoint in Bacillus subtilis. Cell 104 : 269 279.
    • (2001) Cell , vol.104 , pp. 269-279
    • Burkholder, W.F.1    Kurtser, I.2    Grossman, A.D.3
  • 5
    • 0028235205 scopus 로고
    • Benzophenone photophores in biochemistry
    • Dorman, G. Prestwich, G.D. (1994) Benzophenone photophores in biochemistry. Biochemistry 33 : 5661 5673.
    • (1994) Biochemistry , vol.33 , pp. 5661-5673
    • Dorman, G.1    Prestwich, G.D.2
  • 6
    • 1942441039 scopus 로고    scopus 로고
    • Kinetic and mechanistic analyses of new classes of inhibitors of two-component signal transduction systems using a coupled assay containing HpkA-DrrA from Thermotoga maritima
    • Foster, J.E., Sheng, Q., McClain, J.R., Bures, M., Nicas, T.I., Henry, K., et al. (2004) Kinetic and mechanistic analyses of new classes of inhibitors of two-component signal transduction systems using a coupled assay containing HpkA-DrrA from Thermotoga maritima. Microbiology 150 : 885 896.
    • (2004) Microbiology , vol.150 , pp. 885-896
    • Foster, J.E.1    Sheng, Q.2    McClain, J.R.3    Bures, M.4    Nicas, T.I.5    Henry, K.6
  • 7
    • 33645093693 scopus 로고    scopus 로고
    • The putative ABC transporter YheH/YheI is involved in the signalling pathway that activates KinA during sporulation initiation
    • Fukushima, S., Yoshimura, M., Chibazakura, T., Sato, T. Yoshikawa, H. (2006) The putative ABC transporter YheH/YheI is involved in the signalling pathway that activates KinA during sporulation initiation. FEMS Microbiol Lett 256 : 90 97.
    • (2006) FEMS Microbiol Lett , vol.256 , pp. 90-97
    • Fukushima, S.1    Yoshimura, M.2    Chibazakura, T.3    Sato, T.4    Yoshikawa, H.5
  • 9
    • 24644506093 scopus 로고    scopus 로고
    • A transcriptional response to replication status mediated by the conserved bacterial replication protein DnaA
    • Goranov, A.I., Katz, L., Breier, A.M., Burge, C.B. Grossman, A.D. (2005) A transcriptional response to replication status mediated by the conserved bacterial replication protein DnaA. Proc Natl Acad Sci USA 102 : 12932 12937.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 12932-12937
    • Goranov, A.I.1    Katz, L.2    Breier, A.M.3    Burge, C.B.4    Grossman, A.D.5
  • 10
    • 0033277340 scopus 로고    scopus 로고
    • The histidine protein kinase superfamily
    • Grebe, T.W. Stock, J.B. (1999) The histidine protein kinase superfamily. Adv Microb Physiol 41 : 139 227.
    • (1999) Adv Microb Physiol , vol.41 , pp. 139-227
    • Grebe, T.W.1    Stock, J.B.2
  • 11
    • 0032477825 scopus 로고    scopus 로고
    • Synergistic kinetic interactions between components of the phosphorelay controlling sporulation in Bacillus subtilis
    • Grimshaw, C.E., Huang, S., Hanstein, C.G., Strauch, M.A., Burbulys, D., Wang, L., et al. (1998) Synergistic kinetic interactions between components of the phosphorelay controlling sporulation in Bacillus subtilis. Biochemistry 37 : 1365 1375.
    • (1998) Biochemistry , vol.37 , pp. 1365-1375
    • Grimshaw, C.E.1    Huang, S.2    Hanstein, C.G.3    Strauch, M.A.4    Burbulys, D.5    Wang, L.6
  • 12
    • 2942616403 scopus 로고    scopus 로고
    • Compartmentalization of gene expression during Bacillus subtilis spore formation
    • Hilbert, D.W. Piggot, P.J. (2004) Compartmentalization of gene expression during Bacillus subtilis spore formation. Microbiol Mol Biol Rev 68 : 234 262.
    • (2004) Microbiol Mol Biol Rev , vol.68 , pp. 234-262
    • Hilbert, D.W.1    Piggot, P.J.2
  • 13
    • 0031782823 scopus 로고    scopus 로고
    • Mutations that alter the kinase and phosphatase activities of the two-component sensor EnvZ
    • Hsing, W., Russo, F.D., Bernd, K.K. Silhavy, T.J. (1998) Mutations that alter the kinase and phosphatase activities of the two-component sensor EnvZ. J Bacteriol 180 : 4538 4546.
    • (1998) J Bacteriol , vol.180 , pp. 4538-4546
    • Hsing, W.1    Russo, F.D.2    Bernd, K.K.3    Silhavy, T.J.4
  • 14
    • 84902390232 scopus 로고    scopus 로고
    • Pathogenicity and histidine kinases: Approaches toward the development of a new generation of antibiotics
    • In. Inouye, M. Dutta, R. (eds). San Diego, CA: Academic Press, pp.
    • Hubbard, J., Burnham, M.K. Throup, J.P. (2003) Pathogenicity and histidine kinases: approaches toward the development of a new generation of antibiotics. In Histidine Kinases in Signal Transduction. Inouye, M. Dutta, R. (eds). San Diego, CA : Academic Press, pp. 459 481.
    • (2003) Histidine Kinases in Signal Transduction. , pp. 459-481
    • Hubbard, J.1    Burnham, M.K.2    Throup, J.P.3
  • 16
    • 38449109857 scopus 로고    scopus 로고
    • Distribution of stable DnaA-binding sites on the Bacillus subtilis genome detected using a modified ChIP-chip method
    • Ishikawa, S., Ogura, Y., Yoshimura, M., Okumura, H., Cho, E., Kawai, Y., et al. (2007) Distribution of stable DnaA-binding sites on the Bacillus subtilis genome detected using a modified ChIP-chip method. DNA Res 14 : 155 168.
    • (2007) DNA Res , vol.14 , pp. 155-168
    • Ishikawa, S.1    Ogura, Y.2    Yoshimura, M.3    Okumura, H.4    Cho, E.5    Kawai, Y.6
  • 19
    • 44449112421 scopus 로고    scopus 로고
    • Specificity in two-component signal transduction pathways
    • Laub, M.T. Goulian, M. (2007) Specificity in two-component signal transduction pathways. Annu Rev Genet 41 : 121 145.
    • (2007) Annu Rev Genet , vol.41 , pp. 121-145
    • Laub, M.T.1    Goulian, M.2
  • 20
    • 0028942309 scopus 로고
    • Different roles for KinA, KinB, and KinC in the initiation of sporulation in Bacillus subtilis
    • LeDeaux, J.R., Yu, N. Grossman, A.D. (1995) Different roles for KinA, KinB, and KinC in the initiation of sporulation in Bacillus subtilis. J Bacteriol 177 : 861 863.
    • (1995) J Bacteriol , vol.177 , pp. 861-863
    • Ledeaux, J.R.1    Yu, N.2    Grossman, A.D.3
  • 21
    • 0344237413 scopus 로고    scopus 로고
    • Chemical signaling among bacteria and Its inhibition
    • Lyon, G.J. Muir, T.W. (2003) Chemical signaling among bacteria and Its inhibition. Chem Biol 10 : 1007 1021.
    • (2003) Chem Biol , vol.10 , pp. 1007-1021
    • Lyon, G.J.1    Muir, T.W.2
  • 22
    • 0034700175 scopus 로고    scopus 로고
    • Rational design of a global inhibitor of the virulence response in Staphylococcus aureus, based in part on localization of the site of inhibition to the receptor-histidine kinase, AgrC
    • Lyon, G.J., Mayville, P., Muir, T.W. Novick, R.P. (2000) Rational design of a global inhibitor of the virulence response in Staphylococcus aureus, based in part on localization of the site of inhibition to the receptor-histidine kinase, AgrC. Proc Natl Acad Sci USA 97 : 13330 13335.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 13330-13335
    • Lyon, G.J.1    Mayville, P.2    Muir, T.W.3    Novick, R.P.4
  • 23
    • 0033810328 scopus 로고    scopus 로고
    • Inhibitors of bacterial two-component signalling systems
    • Macielag, M.J. Goldschmidt, R. (2000) Inhibitors of bacterial two-component signalling systems. Expert Opin Invest Drugs 9 : 2351 2369.
    • (2000) Expert Opin Invest Drugs , vol.9 , pp. 2351-2369
    • MacIelag, M.J.1    Goldschmidt, R.2
  • 24
    • 29244433095 scopus 로고    scopus 로고
    • Structure of the entire cytoplasmic portion of a sensor histidine-kinase protein
    • Marina, A., Waldburger, C.D. Hendrickson, W.A. (2005) Structure of the entire cytoplasmic portion of a sensor histidine-kinase protein. EMBO J 24 : 4247 4259.
    • (2005) EMBO J , vol.24 , pp. 4247-4259
    • Marina, A.1    Waldburger, C.D.2    Hendrickson, W.A.3
  • 25
    • 33845640610 scopus 로고    scopus 로고
    • Stimulus perception in bacterial signal-transducing histidine kinases
    • Mascher, T., Helmann, J.D. Unden, G. (2006) Stimulus perception in bacterial signal-transducing histidine kinases. Microbiol Mol Biol Rev 70 : 910 938.
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 910-938
    • Mascher, T.1    Helmann, J.D.2    Unden, G.3
  • 26
    • 0036166981 scopus 로고    scopus 로고
    • Histidine kinases as targets for new antimicrobial agents
    • Matsushita, M. Janda, K.D. (2002) Histidine kinases as targets for new antimicrobial agents. Bioorg Med Chem 10 : 855 867.
    • (2002) Bioorg Med Chem , vol.10 , pp. 855-867
    • Matsushita, M.1    Janda, K.D.2
  • 27
    • 34447108830 scopus 로고    scopus 로고
    • Targeting two-component signal transduction: A novel drug discovery system
    • Okada, A., Gotoh, Y., Watanabe, T., Furuta, E., Yamamoto, K. Utsumi, R. (2007) Targeting two-component signal transduction: a novel drug discovery system. Methods Enzymol 422 : 386 395.
    • (2007) Methods Enzymol , vol.422 , pp. 386-395
    • Okada, A.1    Gotoh, Y.2    Watanabe, T.3    Furuta, E.4    Yamamoto, K.5    Utsumi, R.6
  • 28
    • 0032499693 scopus 로고    scopus 로고
    • Two-domain reconstitution of a functional protein histidine kinase
    • Park, H., Saha, S.K. Inouye, M. (1998) Two-domain reconstitution of a functional protein histidine kinase. Proc Natl Acad Sci USA 95 : 6728 6732.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6728-6732
    • Park, H.1    Saha, S.K.2    Inouye, M.3
  • 29
    • 0034830557 scopus 로고    scopus 로고
    • Pentapeptide regulation of aspartyl-phosphate phosphatases
    • Perego, M. Brannigan, J.A. (2001) Pentapeptide regulation of aspartyl-phosphate phosphatases. Peptides 22 : 1541 1547.
    • (2001) Peptides , vol.22 , pp. 1541-1547
    • Perego, M.1    Brannigan, J.A.2
  • 30
    • 34447544806 scopus 로고    scopus 로고
    • Structure-based discovery of inhibitors of the YycG histidine kinase: New chemical leads to combat Staphylococcus epidermidis infections
    • Qin, Z., Zhang, J., Xu, B., Chen, L., Wu, Y., Yang, X., et al. (2006) Structure-based discovery of inhibitors of the YycG histidine kinase: new chemical leads to combat Staphylococcus epidermidis infections. BMC Microbiol 6 : 96.
    • (2006) BMC Microbiol , vol.6 , pp. 96
    • Qin, Z.1    Zhang, J.2    Xu, B.3    Chen, L.4    Wu, Y.5    Yang, X.6
  • 31
    • 1642271608 scopus 로고    scopus 로고
    • Structure and mechanism of action of Sda, an inhibitor of the histidine kinases that regulate initiation of sporulation in Bacillus subtilis
    • Rowland, S.L., Burkholder, W.F., Cunningham, K.A., Maciejewski, M.W., Grossman, A.D. King, G.F. (2004) Structure and mechanism of action of Sda, an inhibitor of the histidine kinases that regulate initiation of sporulation in Bacillus subtilis. Mol Cell 13 : 689 701.
    • (2004) Mol Cell , vol.13 , pp. 689-701
    • Rowland, S.L.1    Burkholder, W.F.2    Cunningham, K.A.3    MacIejewski, M.W.4    Grossman, A.D.5    King, G.F.6
  • 32
    • 36749101070 scopus 로고    scopus 로고
    • Histidine kinases as antimicrobial targets: Prospects and pitfalls
    • Rowland, S.L. King, G.F. (2007) Histidine kinases as antimicrobial targets: prospects and pitfalls. Mini Rev Med Chem 7 : 1144 1154.
    • (2007) Mini Rev Med Chem , vol.7 , pp. 1144-1154
    • Rowland, S.L.1    King, G.F.2
  • 33
    • 33744499965 scopus 로고    scopus 로고
    • Proteolysis of the replication checkpoint protein Sda is necessary for the efficient initiation of sporulation after transient replication stress in Bacillus subtilis
    • Ruvolo, M.V., Mach, K.E. Burkholder, W.F. (2006) Proteolysis of the replication checkpoint protein Sda is necessary for the efficient initiation of sporulation after transient replication stress in Bacillus subtilis. Mol Microbiol 60 : 1490 1508.
    • (2006) Mol Microbiol , vol.60 , pp. 1490-1508
    • Ruvolo, M.V.1    MacH, K.E.2    Burkholder, W.F.3
  • 34
    • 0037163079 scopus 로고    scopus 로고
    • Rapid mapping of protein structure, interactions, and ligand binding by misincorporation proton-alkyl exchange
    • Silverman, J.A. Harbury, P.B. (2002) Rapid mapping of protein structure, interactions, and ligand binding by misincorporation proton-alkyl exchange. J Biol Chem 277 : 30968 30975.
    • (2002) J Biol Chem , vol.277 , pp. 30968-30975
    • Silverman, J.A.1    Harbury, P.B.2
  • 36
    • 33749080319 scopus 로고    scopus 로고
    • Identification of the TRiC/CCT substrate binding sites uncovers the function of subunit diversity in eukaryotic chaperonins
    • Spiess, C., Miller, E.J., McClellan, A.J. Frydman, J. (2006) Identification of the TRiC/CCT substrate binding sites uncovers the function of subunit diversity in eukaryotic chaperonins. Mol Cell 24 : 25 37.
    • (2006) Mol Cell , vol.24 , pp. 25-37
    • Spiess, C.1    Miller, E.J.2    McClellan, A.J.3    Frydman, J.4
  • 37
    • 1642309791 scopus 로고    scopus 로고
    • Developing inhibitors to selectively target two-component and phosphorelay signal transduction systems of pathogenic microorganisms
    • Stephenson, K. Hoch, J.A. (2004) Developing inhibitors to selectively target two-component and phosphorelay signal transduction systems of pathogenic microorganisms. Curr Med Chem 11 : 765 773.
    • (2004) Curr Med Chem , vol.11 , pp. 765-773
    • Stephenson, K.1    Hoch, J.A.2
  • 39
    • 48249148736 scopus 로고    scopus 로고
    • Co-evolving motions at protein-protein interfaces of two-component signaling systems identified by covariance analysis
    • Szurmant, H., Bobay, B.G., White, R.A., Sullivan, D.M., Thompson, R.J., Hwa, T., et al. (2008) Co-evolving motions at protein-protein interfaces of two-component signaling systems identified by covariance analysis. Biochemistry 47 : 7782 7784.
    • (2008) Biochemistry , vol.47 , pp. 7782-7784
    • Szurmant, H.1    Bobay, B.G.2    White, R.A.3    Sullivan, D.M.4    Thompson, R.J.5    Hwa, T.6
  • 40
    • 0032804404 scopus 로고    scopus 로고
    • Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ
    • Tomomori, C., Tanaka, T., Dutta, R., Park, H., Saha, S.K., Zhu, Y., et al. (1999) Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ. Nat Struct Biol 6 : 729 734.
    • (1999) Nat Struct Biol , vol.6 , pp. 729-734
    • Tomomori, C.1    Tanaka, T.2    Dutta, R.3    Park, H.4    Saha, S.K.5    Zhu, Y.6
  • 41
    • 0027474353 scopus 로고
    • Multisensory activation of the phosphorelay initiating sporulation in Bacillus subtilis: Identification and sequence of the protein kinase of the alternate pathway
    • Trach, K.A. Hoch, J.A. (1993) Multisensory activation of the phosphorelay initiating sporulation in Bacillus subtilis: identification and sequence of the protein kinase of the alternate pathway. Mol Microbiol 8 : 69 79.
    • (1993) Mol Microbiol , vol.8 , pp. 69-79
    • Trach, K.A.1    Hoch, J.A.2
  • 42
    • 84902405080 scopus 로고    scopus 로고
    • Signal transmission and specificity in the sporulation phosphorelay of Bacillus subtilis
    • In. Inouye, M. Dutta, R. (eds). Amsterdam: Academic Press, pp.
    • Varughese, K.I. (2003) Signal transmission and specificity in the sporulation phosphorelay of Bacillus subtilis. In Histidine Kinases in Signal Transduction. Inouye, M. Dutta, R. (eds). Amsterdam : Academic Press, pp. 203 218.
    • (2003) Histidine Kinases in Signal Transduction. , pp. 203-218
    • Varughese, K.I.1
  • 43
    • 0030764211 scopus 로고    scopus 로고
    • A novel histidine kinase inhibitor regulating development in Bacillus subtilis
    • Wang, L., Grau, R., Perego, M. Hoch, J.A. (1997) A novel histidine kinase inhibitor regulating development in Bacillus subtilis. Genes Dev 11 : 2569 2579.
    • (1997) Genes Dev , vol.11 , pp. 2569-2579
    • Wang, L.1    Grau, R.2    Perego, M.3    Hoch, J.A.4
  • 44
    • 34447104524 scopus 로고    scopus 로고
    • Features of protein-protein interactions in two-component signaling deduced from genomic libraries
    • White, R.A., Szurmant, H., Hoch, J.A. Hwa, T. (2007) Features of protein-protein interactions in two-component signaling deduced from genomic libraries. Methods Enzymol 422 : 75 101.
    • (2007) Methods Enzymol , vol.422 , pp. 75-101
    • White, R.A.1    Szurmant, H.2    Hoch, J.A.3    Hwa, T.4
  • 45
    • 33947638546 scopus 로고    scopus 로고
    • The structure of the KinA-Sda complex suggests an allosteric mechanism of histidine kinase inhibition
    • Whitten, A.E., Jacques, D.A., Hammouda, B., Hanley, T., King, G.F., Guss, J.M., et al. (2007) The structure of the KinA-Sda complex suggests an allosteric mechanism of histidine kinase inhibition. J Mol Biol 368 : 407 420.
    • (2007) J Mol Biol , vol.368 , pp. 407-420
    • Whitten, A.E.1    Jacques, D.A.2    Hammouda, B.3    Hanley, T.4    King, G.F.5    Guss, J.M.6
  • 46
    • 0034662751 scopus 로고    scopus 로고
    • A transient interaction between two phosphorelay proteins trapped in a crystal lattice reveals the mechanism of molecular recognition and phosphotransfer in signal transduction
    • Zapf, J., Sen, U., Madhusudan, Hoch, J.A. Varughese, K.I. (2000) A transient interaction between two phosphorelay proteins trapped in a crystal lattice reveals the mechanism of molecular recognition and phosphotransfer in signal transduction. Struct Fold Des 8 : 851 862.
    • (2000) Struct Fold des , vol.8 , pp. 851-862
    • Zapf, J.1    Sen, U.2    Madhusudan3    Hoch, J.A.4    Varughese, K.I.5


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