메뉴 건너뛰기




Volumn 12, Issue 10, 2014, Pages

Cell Fate Regulation Governed by a Repurposed Bacterial Histidine Kinase

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; DIVK PROTEIN; DIVL PROTEIN; PHOSPHATASE; PROTEIN HISTIDINE KINASE; REGULATOR PROTEIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR CTRA; UNCLASSIFIED DRUG; DIVK PROTEIN, CAULOBACTER CRESCENTUS; PROTEIN BINDING; PROTEIN KINASE; PROTEIN-HISTIDINE KINASE;

EID: 84920455185     PISSN: 15449173     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.1001979     Document Type: Article
Times cited : (55)

References (67)
  • 2
    • 26444490066 scopus 로고    scopus 로고
    • Distinct constrictive processes, separated in time and space, divide caulobacter inner and outer membranes
    • Judd EM, Comolli LR, Chen JC, Downing KH, Moerner WE, et al. (2005) Distinct constrictive processes, separated in time and space, divide caulobacter inner and outer membranes. J Bacteriol 187: 6874–6882.
    • (2005) J Bacteriol , vol.187 , pp. 6874-6882
    • Judd, E.M.1    Comolli, L.R.2    Chen, J.C.3    Downing, K.H.4    Moerner, W.E.5
  • 3
    • 0037816244 scopus 로고    scopus 로고
    • Fluorescence bleaching reveals asymmetric compartment formation prior to cell division in Caulobacter
    • Judd EM, Ryan KR, Moerner WE, Shapiro L, McAdams HH, (2003) Fluorescence bleaching reveals asymmetric compartment formation prior to cell division in Caulobacter. Proc Natl Acad Sci U S A 100: 8235–8240.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 8235-8240
    • Judd, E.M.1    Ryan, K.R.2    Moerner, W.E.3    Shapiro, L.4    McAdams, H.H.5
  • 4
    • 0033231550 scopus 로고    scopus 로고
    • Differential localization of two histidine kinases controlling bacterial cell differentiation
    • Wheeler RT, Shapiro L, (1999) Differential localization of two histidine kinases controlling bacterial cell differentiation. Mol Cell 4: 683–694.
    • (1999) Mol Cell , vol.4 , pp. 683-694
    • Wheeler, R.T.1    Shapiro, L.2
  • 5
    • 4444372637 scopus 로고    scopus 로고
    • Cytokinesis monitoring during development; rapid pole-to-pole shuttling of a signaling protein by localized kinase and phosphatase in Caulobacter
    • Matroule JY, Lam H, Burnette DT, Jacobs-Wagner C, (2004) Cytokinesis monitoring during development; rapid pole-to-pole shuttling of a signaling protein by localized kinase and phosphatase in Caulobacter. Cell 118: 579–590.
    • (2004) Cell , vol.118 , pp. 579-590
    • Matroule, J.Y.1    Lam, H.2    Burnette, D.T.3    Jacobs-Wagner, C.4
  • 6
    • 2442531895 scopus 로고    scopus 로고
    • Recruitment of a cytoplasmic response regulator to the cell pole is linked to its cell cycle-regulated proteolysis
    • Ryan KR, Huntwork S, Shapiro L, (2004) Recruitment of a cytoplasmic response regulator to the cell pole is linked to its cell cycle-regulated proteolysis. Proc Natl Acad Sci U S A 101: 7415–7420.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 7415-7420
    • Ryan, K.R.1    Huntwork, S.2    Shapiro, L.3
  • 7
    • 0037007079 scopus 로고    scopus 로고
    • Genes directly controlled by CtrA, a master regulator of the Caulobacter cell cycle
    • Laub MT, Chen SL, Shapiro L, McAdams HH, (2002) Genes directly controlled by CtrA, a master regulator of the Caulobacter cell cycle. Proc Natl Acad Sci U S A 99: 4632–4637.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 4632-4637
    • Laub, M.T.1    Chen, S.L.2    Shapiro, L.3    McAdams, H.H.4
  • 8
    • 84866065165 scopus 로고    scopus 로고
    • Interplay between the localization and kinetics of phosphorylation in flagellar pole development of the bacterium Caulobacter crescentus
    • Tropini C, Huang KC, (2012) Interplay between the localization and kinetics of phosphorylation in flagellar pole development of the bacterium Caulobacter crescentus. PLoS Comput Biol 8: e1002602.
    • (2012) PLoS Comput Biol , vol.8 , pp. e1002602
    • Tropini, C.1    Huang, K.C.2
  • 9
    • 42949140533 scopus 로고    scopus 로고
    • Allosteric regulation of histidine kinases by their cognate response regulator determines cell fate
    • Paul R, Jaeger T, Abel S, Wiederkehr I, Folcher M, et al. (2008) Allosteric regulation of histidine kinases by their cognate response regulator determines cell fate. Cell 133: 452–461.
    • (2008) Cell , vol.133 , pp. 452-461
    • Paul, R.1    Jaeger, T.2    Abel, S.3    Wiederkehr, I.4    Folcher, M.5
  • 10
    • 0038686494 scopus 로고    scopus 로고
    • The asymmetric spatial distribution of bacterial signal transduction proteins coordinates cell cycle events
    • Lam H, Matroule JY, Jacobs-Wagner C, (2003) The asymmetric spatial distribution of bacterial signal transduction proteins coordinates cell cycle events. Dev Cell 5: 149–159.
    • (2003) Dev Cell , vol.5 , pp. 149-159
    • Lam, H.1    Matroule, J.Y.2    Jacobs-Wagner, C.3
  • 11
    • 0035957365 scopus 로고    scopus 로고
    • Dynamic localization of a cytoplasmic signal transduction response regulator controls morphogenesis during the Caulobacter cell cycle
    • Jacobs C, Hung D, Shapiro L, (2001) Dynamic localization of a cytoplasmic signal transduction response regulator controls morphogenesis during the Caulobacter cell cycle. Proc Natl Acad Sci U S A 98: 4095–4100.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 4095-4100
    • Jacobs, C.1    Hung, D.2    Shapiro, L.3
  • 12
    • 36549065749 scopus 로고    scopus 로고
    • DivL performs critical cell cycle functions in Caulobacter crescentus independent of kinase activity
    • Reisinger SJ, Huntwork S, Viollier PH, Ryan KR, (2007) DivL performs critical cell cycle functions in Caulobacter crescentus independent of kinase activity. J Bacteriol 189: 8308–8320.
    • (2007) J Bacteriol , vol.189 , pp. 8308-8320
    • Reisinger, S.J.1    Huntwork, S.2    Viollier, P.H.3    Ryan, K.R.4
  • 13
    • 79952500685 scopus 로고    scopus 로고
    • A dynamic complex of signaling proteins uses polar localization to regulate cell-fate asymmetry in Caulobacter crescentus
    • Tsokos CG, Perchuk BS, Laub MT, (2011) A dynamic complex of signaling proteins uses polar localization to regulate cell-fate asymmetry in Caulobacter crescentus. Dev Cell 20: 329–341.
    • (2011) Dev Cell , vol.20 , pp. 329-341
    • Tsokos, C.G.1    Perchuk, B.S.2    Laub, M.T.3
  • 14
    • 0037767533 scopus 로고    scopus 로고
    • The core dimerization domains of histidine kinases contain recognition specificity for the cognate response regulator
    • Ohta N, Newton A, (2003) The core dimerization domains of histidine kinases contain recognition specificity for the cognate response regulator. J Bacteriol 185: 4424–4431.
    • (2003) J Bacteriol , vol.185 , pp. 4424-4431
    • Ohta, N.1    Newton, A.2
  • 15
    • 55949128346 scopus 로고    scopus 로고
    • A bacterial control circuit integrates polar localization and proteolysis of key regulatory proteins with a phospho-signaling cascade
    • Iniesta AA, Shapiro L, (2008) A bacterial control circuit integrates polar localization and proteolysis of key regulatory proteins with a phospho-signaling cascade. Proc Natl Acad Sci U S A 105: 16602–16607.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 16602-16607
    • Iniesta, A.A.1    Shapiro, L.2
  • 16
    • 77951029841 scopus 로고    scopus 로고
    • Cell pole-specific activation of a critical bacterial cell cycle kinase
    • Iniesta AA, Hillson NJ, Shapiro L, (2010) Cell pole-specific activation of a critical bacterial cell cycle kinase. Proc Natl Acad Sci U S A 107: 7012–7017.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 7012-7017
    • Iniesta, A.A.1    Hillson, N.J.2    Shapiro, L.3
  • 17
    • 0033539643 scopus 로고    scopus 로고
    • A novel bacterial tyrosine kinase essential for cell division and differentiation
    • Wu JG, Ohta N, Zhao JL, Newton A, (1999) A novel bacterial tyrosine kinase essential for cell division and differentiation. Proc Natl Acad Sci U S A 96: 13068–13073.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 13068-13073
    • Wu, J.G.1    Ohta, N.2    Zhao, J.L.3    Newton, A.4
  • 19
    • 77951601819 scopus 로고    scopus 로고
    • The diversity and evolution of cell cycle regulation in alpha-proteobacteria: a comparative genomic analysis
    • Brilli M, Fondi M, Fani R, Mengoni A, Ferri L, et al. (2010) The diversity and evolution of cell cycle regulation in alpha-proteobacteria: a comparative genomic analysis. BMC Syst Biol 4.
    • (2010) BMC Syst Biol , vol.4
    • Brilli, M.1    Fondi, M.2    Fani, R.3    Mengoni, A.4    Ferri, L.5
  • 20
    • 0037192777 scopus 로고    scopus 로고
    • Phosphorylation alters the interaction of the response regulator OmpR with its sensor kinase EnvZ
    • Mattison K, Kenney LJ, (2002) Phosphorylation alters the interaction of the response regulator OmpR with its sensor kinase EnvZ. J Biol Chem 277: 11143–11148.
    • (2002) J Biol Chem , vol.277 , pp. 11143-11148
    • Mattison, K.1    Kenney, L.J.2
  • 21
    • 84891612853 scopus 로고    scopus 로고
    • Specificity residues determine binding affinity for two-component signal transduction systems
    • Willett JW, Tiwari N, Muller S, Hummels KR, Houtman JC, et al. (2013) Specificity residues determine binding affinity for two-component signal transduction systems. MBio 4: e00420–00413.
    • (2013) MBio , vol.4 , pp. 00413-00420
    • Willett, J.W.1    Tiwari, N.2    Muller, S.3    Hummels, K.R.4    Houtman, J.C.5
  • 23
    • 70349795241 scopus 로고    scopus 로고
    • Structural insight into partner specificity and phosphoryl transfer in two-component signal transduction
    • Casino P, Rubio V, Marina A, (2009) Structural insight into partner specificity and phosphoryl transfer in two-component signal transduction. Cell 139: 325–336.
    • (2009) Cell , vol.139 , pp. 325-336
    • Casino, P.1    Rubio, V.2    Marina, A.3
  • 24
    • 29244433095 scopus 로고    scopus 로고
    • Structure of the entire cytoplasmic portion of a sensor histidine-kinase protein
    • Marina A, Waldburger CD, Hendrickson WA, (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
    • 70349764676 scopus 로고    scopus 로고
    • Structure of PAS-linked histidine kinase and the response regulator complex
    • Yamada S, Sugimoto H, Kobayashi M, Ohno A, Nakamura H, et al. (2009) Structure of PAS-linked histidine kinase and the response regulator complex. Structure 17: 1333–1344.
    • (2009) Structure , vol.17 , pp. 1333-1344
    • Yamada, S.1    Sugimoto, H.2    Kobayashi, M.3    Ohno, A.4    Nakamura, H.5
  • 26
    • 84874684844 scopus 로고    scopus 로고
    • Mechanistic insights revealed by the crystal structure of a histidine kinase with signal transducer and sensor domains
    • Wang C, Sang J, Wang J, Su M, Downey JS, et al. (2013) Mechanistic insights revealed by the crystal structure of a histidine kinase with signal transducer and sensor domains. PLoS Biol 11: e1001493.
    • (2013) PLoS Biol , vol.11 , pp. e1001493
    • Wang, C.1    Sang, J.2    Wang, J.3    Su, M.4    Downey, J.S.5
  • 27
    • 84893827341 scopus 로고    scopus 로고
    • Visualizing autophosphorylation in histidine kinases
    • Casino P, Miguel-Romero L, Marina A, (2014) Visualizing autophosphorylation in histidine kinases. Nat Commun 5: 3258.
    • (2014) Nat Commun , vol.5 , pp. 3258
    • Casino, P.1    Miguel-Romero, L.2    Marina, A.3
  • 28
    • 84879836986 scopus 로고    scopus 로고
    • Full-length structure of a sensor histidine kinase pinpoints coaxial coiled coils as signal transducers and modulators
    • Diensthuber RP, Bommer M, Gleichmann T, Moglich A, (2013) Full-length structure of a sensor histidine kinase pinpoints coaxial coiled coils as signal transducers and modulators. Structure 21: 1127–1136.
    • (2013) Structure , vol.21 , pp. 1127-1136
    • Diensthuber, R.P.1    Bommer, M.2    Gleichmann, T.3    Moglich, A.4
  • 29
    • 33748585939 scopus 로고    scopus 로고
    • Ligand-induced asymmetry in histidine sensor kinase complex regulates quorum sensing
    • Neiditch MB, Federle MJ, Pompeani AJ, Kelly RC, Swem DL, et al. (2006) Ligand-induced asymmetry in histidine sensor kinase complex regulates quorum sensing. Cell 126: 1095–1108.
    • (2006) Cell , vol.126 , pp. 1095-1108
    • Neiditch, M.B.1    Federle, M.J.2    Pompeani, A.J.3    Kelly, R.C.4    Swem, D.L.5
  • 30
    • 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 JA, Varughese KI, (2000) A transient interaction between two phosphorelay proteins trapped in a crystal lattice reveals the mechanism of molecular recognition and phosphotransfer in signal transduction. Structure 8: 851–862.
    • (2000) Structure , vol.8 , pp. 851-862
    • Zapf, J.1    Sen, U.2    Madhusudan, Hoch, J.A.3    Varughese, K.I.4
  • 31
    • 58849159963 scopus 로고    scopus 로고
    • How to switch off a histidine kinase: crystal structure of Geobacillus stearothermophilus KinB with the inhibitor Sda
    • Bick MJ, Lamour V, Rajashankar KR, Gordiyenko Y, Robinson CV, et al. (2009) How to switch off a histidine kinase: crystal structure of Geobacillus stearothermophilus KinB with the inhibitor Sda. J Mol Biol 386: 163–177.
    • (2009) J Mol Biol , vol.386 , pp. 163-177
    • Bick, M.J.1    Lamour, V.2    Rajashankar, K.R.3    Gordiyenko, Y.4    Robinson, C.V.5
  • 32
    • 84893731658 scopus 로고    scopus 로고
    • Segmental helical motions and dynamical asymmetry modulate histidine kinase autophosphorylation
    • Mechaly AE, Sassoon N, Betton JM, Alzari PM, (2014) Segmental helical motions and dynamical asymmetry modulate histidine kinase autophosphorylation. PLoS Biol 12: e1001776.
    • (2014) PLoS Biol , vol.12 , pp. e1001776
    • Mechaly, A.E.1    Sassoon, N.2    Betton, J.M.3    Alzari, P.M.4
  • 33
    • 84863006375 scopus 로고    scopus 로고
    • Structural basis of histidine kinase autophosphorylation deduced by integrating genomics, molecular dynamics, and mutagenesis
    • Dago AE, Schug A, Procaccini A, Hoch JA, Weigt M, et al. (2012) Structural basis of histidine kinase autophosphorylation deduced by integrating genomics, molecular dynamics, and mutagenesis. Proc Natl Acad Sci U S A 109: E1733–1742.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 1733-1742
    • Dago, A.E.1    Schug, A.2    Procaccini, A.3    Hoch, J.A.4    Weigt, M.5
  • 34
    • 0032168668 scopus 로고    scopus 로고
    • TNP-ATP and TNP-ADP as probes of the nucleotide binding site of CheA, the histidine protein kinase in the chemotaxis signal transduction pathway of Escherichia coli
    • Stewart RC, VanBruggen R, Ellefson DD, Wolfe AJ, (1998) TNP-ATP and TNP-ADP as probes of the nucleotide binding site of CheA, the histidine protein kinase in the chemotaxis signal transduction pathway of Escherichia coli. Biochemistry 37: 12269–12279.
    • (1998) Biochemistry , vol.37 , pp. 12269-12279
    • Stewart, R.C.1    VanBruggen, R.2    Ellefson, D.D.3    Wolfe, A.J.4
  • 35
    • 27944506452 scopus 로고    scopus 로고
    • Oxygen blocks the reaction of the FixL-FixJ complex with ATP but does not influence binding of FixJ or ATP to FixL
    • Sousa EH, Gonzalez G, Gilles-Gonzalez MA, (2005) Oxygen blocks the reaction of the FixL-FixJ complex with ATP but does not influence binding of FixJ or ATP to FixL. Biochemistry 44: 15359–15365.
    • (2005) Biochemistry , vol.44 , pp. 15359-15365
    • Sousa, E.H.1    Gonzalez, G.2    Gilles-Gonzalez, M.A.3
  • 36
    • 0037180380 scopus 로고    scopus 로고
    • Probing the nucleotide binding domain of the osmoregulator EnvZ using fluorescent nucleotide derivatives
    • Plesniak L, Horiuchi Y, Sem D, Meinenger D, Stiles L, et al. (2002) Probing the nucleotide binding domain of the osmoregulator EnvZ using fluorescent nucleotide derivatives. Biochemistry 41: 13876–13882.
    • (2002) Biochemistry , vol.41 , pp. 13876-13882
    • Plesniak, L.1    Horiuchi, Y.2    Sem, D.3    Meinenger, D.4    Stiles, L.5
  • 37
    • 34247170877 scopus 로고    scopus 로고
    • Probing the nucleotide binding and phosphorylation by the histidine kinase of a novel three-protein two-component system from Mycobacterium tuberculosis
    • Shrivastava R, Ghosh AK, Das AK, (2007) Probing the nucleotide binding and phosphorylation by the histidine kinase of a novel three-protein two-component system from Mycobacterium tuberculosis. FEBS Lett 581: 1903–1909.
    • (2007) FEBS Lett , vol.581 , pp. 1903-1909
    • Shrivastava, R.1    Ghosh, A.K.2    Das, A.K.3
  • 38
    • 79953779836 scopus 로고    scopus 로고
    • A high-throughput TNP-ATP displacement assay for screening inhibitors of ATP-binding in bacterial histidine kinases
    • Guarnieri MT, Blagg BS, Zhao R, (2011) A high-throughput TNP-ATP displacement assay for screening inhibitors of ATP-binding in bacterial histidine kinases. Assay Drug Dev Technol 9: 174–183.
    • (2011) Assay Drug Dev Technol , vol.9 , pp. 174-183
    • Guarnieri, M.T.1    Blagg, B.S.2    Zhao, R.3
  • 39
    • 77955291575 scopus 로고    scopus 로고
    • Polar remodeling and histidine kinase activation, which is essential for caulobacter cell cycle progression, are dependent on DNA replication initiation
    • Iniesta AA, Hillson NJ, Shapiro L, (2010) Polar remodeling and histidine kinase activation, which is essential for caulobacter cell cycle progression, are dependent on DNA replication initiation. J Bacteriol 192: 3893–3902.
    • (2010) J Bacteriol , vol.192 , pp. 3893-3902
    • Iniesta, A.A.1    Hillson, N.J.2    Shapiro, L.3
  • 40
    • 36749049715 scopus 로고    scopus 로고
    • A comprehensive set of plasmids for vanillate- and xylose-inducible gene expression in Caulobacter crescentus
    • Thanbichler M, Iniesta AA, Shapiro L, (2007) A comprehensive set of plasmids for vanillate- and xylose-inducible gene expression in Caulobacter crescentus. Nucleic Acids Res 35.
    • (2007) Nucleic Acids Res , vol.35
    • Thanbichler, M.1    Iniesta, A.A.2    Shapiro, L.3
  • 41
    • 58549114185 scopus 로고    scopus 로고
    • Identification of direct residue contacts in protein-protein interaction by message passing
    • Weigt M, White RA, Szurmant H, Hoch JA, Hwa T, (2009) Identification of direct residue contacts in protein-protein interaction by message passing. Proc Natl Acad Sci U S A 106: 67–72.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 67-72
    • Weigt, M.1    White, R.A.2    Szurmant, H.3    Hoch, J.A.4    Hwa, T.5
  • 42
    • 34447104524 scopus 로고    scopus 로고
    • Features of protein-protein interactions in two-component signaling deduced from genomic libraries
    • White RA, Szurmant H, Hoch JA, 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
  • 43
    • 78649704332 scopus 로고    scopus 로고
    • Systematic dissection and trajectory-scanning mutagenesis of the molecular interface that ensures specificity of two-component signaling pathways
    • Capra EJ, Perchuk BS, Lubin EA, Ashenberg O, Skerker JM, et al. (2010) Systematic dissection and trajectory-scanning mutagenesis of the molecular interface that ensures specificity of two-component signaling pathways. PLoS Genet 6: e1001220.
    • (2010) PLoS Genet , vol.6 , pp. e1001220
    • Capra, E.J.1    Perchuk, B.S.2    Lubin, E.A.3    Ashenberg, O.4    Skerker, J.M.5
  • 44
    • 44649153450 scopus 로고    scopus 로고
    • Rewiring the specificity of two-component signal transduction systems
    • Skerker JM, Perchuk BS, Siryaporn A, Lubin EA, Ashenberg O, et al. (2008) Rewiring the specificity of two-component signal transduction systems. Cell 133: 1043–1054.
    • (2008) Cell , vol.133 , pp. 1043-1054
    • Skerker, J.M.1    Perchuk, B.S.2    Siryaporn, A.3    Lubin, E.A.4    Ashenberg, O.5
  • 45
    • 84883486987 scopus 로고    scopus 로고
    • Branched signal wiring of an essential bacterial cell-cycle phosphotransfer protein
    • Blair JA, Xu Q, Childers WS, Mathews II, Kern JW, et al. (2013) Branched signal wiring of an essential bacterial cell-cycle phosphotransfer protein. Structure 21: 1590–1601.
    • (2013) Structure , vol.21 , pp. 1590-1601
    • Blair, J.A.1    Xu, Q.2    Childers, W.S.3    Mathews, I.I.4    Kern, J.W.5
  • 46
    • 77951033959 scopus 로고    scopus 로고
    • Kinetic characterization of the WalRKSpn (VicRK) two-component system of Streptococcus pneumoniae: dependence of WalKSpn (VicK) phosphatase activity on its PAS domain
    • Gutu AD, Wayne KJ, Sham LT, Winkler ME, (2010) Kinetic characterization of the WalRKSpn (VicRK) two-component system of Streptococcus pneumoniae: dependence of WalKSpn (VicK) phosphatase activity on its PAS domain. J Bacteriol 192: 2346–2358.
    • (2010) J Bacteriol , vol.192 , pp. 2346-2358
    • Gutu, A.D.1    Wayne, K.J.2    Sham, L.T.3    Winkler, M.E.4
  • 47
    • 84896375166 scopus 로고    scopus 로고
    • Activation and inhibition of the receptor histidine kinase AgrC occurs through opposite helical transduction motions
    • Wang B, Zhao A, Novick RP, Muir TW, (2014) Activation and inhibition of the receptor histidine kinase AgrC occurs through opposite helical transduction motions. Mol Cell 53: 929–940.
    • (2014) Mol Cell , vol.53 , pp. 929-940
    • Wang, B.1    Zhao, A.2    Novick, R.P.3    Muir, T.W.4
  • 48
  • 49
    • 34547820278 scopus 로고    scopus 로고
    • Integration of rotation and piston motions in coiled-coil signal transduction
    • Gao R, Lynn DG, (2007) Integration of rotation and piston motions in coiled-coil signal transduction. J Bacteriol 189: 6048–6056.
    • (2007) J Bacteriol , vol.189 , pp. 6048-6056
    • Gao, R.1    Lynn, D.G.2
  • 50
    • 84901041904 scopus 로고    scopus 로고
    • Role of the VirA histidine autokinase of Agrobacterium tumefaciens in the initial steps of pathogenesis
    • Lin Y-H, Pierce BD, Fang F, Wise A, Binns A, et al. (2014) Role of the VirA histidine autokinase of Agrobacterium tumefaciens in the initial steps of pathogenesis. Front Plant Sci 5: 195.
    • (2014) Front Plant Sci , vol.5 , pp. 195
    • Lin, Y.-H.1    Pierce, B.D.2    Fang, F.3    Wise, A.4    Binns, A.5
  • 51
    • 67650079187 scopus 로고    scopus 로고
    • The two active sites of Thermotoga maritima CheA dimers bind ATP with dramatically different affinities
    • Eaton AK, Stewart RC, (2009) The two active sites of Thermotoga maritima CheA dimers bind ATP with dramatically different affinities. Biochemistry 48: 6412–6422.
    • (2009) Biochemistry , vol.48 , pp. 6412-6422
    • Eaton, A.K.1    Stewart, R.C.2
  • 52
    • 33645220774 scopus 로고    scopus 로고
    • Mutations in DivL and CckA rescue a divJ null mutant of Caulobacter crescentus by reducing the activity of CtrA
    • Pierce DL, O'Donnol DS, Allen RC, Javens JW, Quardokus EM, et al. (2006) Mutations in DivL and CckA rescue a divJ null mutant of Caulobacter crescentus by reducing the activity of CtrA. J Bacteriol 188: 2473–2482.
    • (2006) J Bacteriol , vol.188 , pp. 2473-2482
    • Pierce, D.L.1    O'Donnol, D.S.2    Allen, R.C.3    Javens, J.W.4    Quardokus, E.M.5
  • 53
    • 33845870386 scopus 로고    scopus 로고
    • Regulation of the bacterial cell cycle by an integrated genetic circuit
    • Biondi EG, Reisinger SJ, Skerker JM, Arif M, Perchuk BS, et al. (2006) Regulation of the bacterial cell cycle by an integrated genetic circuit. Nature 444: 899–904.
    • (2006) Nature , vol.444 , pp. 899-904
    • Biondi, E.G.1    Reisinger, S.J.2    Skerker, J.M.3    Arif, M.4    Perchuk, B.S.5
  • 54
    • 23144452044 scopus 로고    scopus 로고
    • The HHpred interactive server for protein homology detection and structure prediction
    • Soding J, Biegert A, Lupas AN, (2005) The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Res 33: W244–W248.
    • (2005) Nucleic Acids Res , vol.33 , pp. W244-W248
    • Soding, J.1    Biegert, A.2    Lupas, A.N.3
  • 56
    • 37549039510 scopus 로고    scopus 로고
    • A short history of SHELX
    • Sheldrick GM, (2008) A short history of SHELX. Acta Crystallogr A 64: 112–122.
    • (2008) Acta Crystallogr A , vol.64 , pp. 112-122
    • Sheldrick, G.M.1
  • 58
    • 33748337934 scopus 로고    scopus 로고
    • The Buccaneer software for automated model building. 1. Tracing protein chains
    • Cowtan K, (2006) The Buccaneer software for automated model building. 1. Tracing protein chains. Acta Crystallogr D Biol Crystallogr 62: 1002–1011.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 1002-1011
    • Cowtan, K.1
  • 59
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K, (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60: 2126–2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 60
    • 85081867430 scopus 로고    scopus 로고
    • Bricogne G, Blanc E, Brandl M, Flensburg C, Keller P, et al. (2011) BUSTER. 2.10.0 ed. Cambridge, United Kingdom: Global Phasing Ltd.
  • 61
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project No. 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
  • 62
    • 83355171249 scopus 로고    scopus 로고
    • An SMC ATPase mutant disrupts chromosome segregation in Caulobacter
    • Schwartz MA, Shapiro L, (2011) An SMC ATPase mutant disrupts chromosome segregation in Caulobacter. Mol Microbiol 82: 1359–1374.
    • (2011) Mol Microbiol , vol.82 , pp. 1359-1374
    • Schwartz, M.A.1    Shapiro, L.2
  • 63
    • 0141737560 scopus 로고    scopus 로고
    • NADH-coupled microplate photometric assay for kinetic studies of ATP-hydrolyzing enzymes with low and high specific activities
    • Kiianitsa K, Solinger JA, Heyer WD, (2003) NADH-coupled microplate photometric assay for kinetic studies of ATP-hydrolyzing enzymes with low and high specific activities. Anal Biochem 321: 266–271.
    • (2003) Anal Biochem , vol.321 , pp. 266-271
    • Kiianitsa, K.1    Solinger, J.A.2    Heyer, W.D.3
  • 64
    • 0035227959 scopus 로고    scopus 로고
    • Use of a real-time, coupled assay to measure the ATPase activity of DNA topoisomerase II
    • Lindsley J, (2001) Use of a real-time, coupled assay to measure the ATPase activity of DNA topoisomerase II. Methods Mol Biol 95: 57–64.
    • (2001) Methods Mol Biol , vol.95 , pp. 57-64
    • Lindsley, J.1
  • 65
    • 0014266489 scopus 로고
    • Binding of guanosine 5′-triphosphate by soluble factors required for polypeptide synthesis
    • Ertel R, Brot N, Redfield B, Allende JE, Weissbach H, (1968) Binding of guanosine 5′-triphosphate by soluble factors required for polypeptide synthesis. Proc Natl Acad Sci U S A 59: 861–868.
    • (1968) Proc Natl Acad Sci U S A , vol.59 , pp. 861-868
    • Ertel, R.1    Brot, N.2    Redfield, B.3    Allende, J.E.4    Weissbach, H.5
  • 66
    • 0016017013 scopus 로고
    • Elongation factor Tu and the aminoacyl-tRNA-EFTu-GTP complex
    • Miller DL, Weissbach H, (1974) Elongation factor Tu and the aminoacyl-tRNA-EFTu-GTP complex. Methods Enzymol 30: 219–232.
    • (1974) Methods Enzymol , vol.30 , pp. 219-232
    • Miller, D.L.1    Weissbach, H.2
  • 67
    • 0027056677 scopus 로고
    • Communication modules in bacterial signaling proteins
    • Parkinson JS, Kofoid EC, (1992) Communication modules in bacterial signaling proteins. Annu Rev Genet 26: 71–112.
    • (1992) Annu Rev Genet , vol.26 , pp. 71-112
    • Parkinson, J.S.1    Kofoid, E.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.