메뉴 건너뛰기




Volumn 19, Issue 4, 2011, Pages 577-587

Structural insights into Rcs phosphotransfer: The newly identified RcsD-ABL domain enhances interaction with the response regulator RcsB

Author keywords

[No Author keywords available]

Indexed keywords

ABELSON KINASE; HISTIDINE PHOSPHOTRANSFERASE; PHOSPHOTRANSFERASE; RCS PHOSPHOTRANSFER; RCSD ABL PROTEIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR RCSB; TRANSCRIPTION FACTOR RCSD; UNCLASSIFIED DRUG;

EID: 79953871014     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2011.01.012     Document Type: Article
Times cited : (15)

References (57)
  • 2
    • 77649085253 scopus 로고    scopus 로고
    • Using structural information to change the phosphotransfer specificity of a two-component chemotaxis signalling complex
    • C.H. Bell, S.L. Porter, A. Strawson, D.I. Stuart, and J.P. Armitage Using structural information to change the phosphotransfer specificity of a two-component chemotaxis signalling complex PLoS Biol. 8 2010 e1000306
    • (2010) PLoS Biol. , vol.8 , pp. 1000306
    • Bell, C.H.1    Porter, S.L.2    Strawson, A.3    Stuart, D.I.4    Armitage, J.P.5
  • 3
    • 0033534368 scopus 로고    scopus 로고
    • Structure of CheA, a signal-transducing histidine kinase
    • DOI 10.1016/S0092-8674(00)80966-6
    • A.M. Bilwes, L.A. Alex, B.R. Crane, and M.I. Simon Structure of CheA, a signal-transducing histidine kinase Cell 96 1999 131 141 (Pubitemid 29044160)
    • (1999) Cell , vol.96 , Issue.1 , pp. 131-141
    • Bilwes, A.M.1    Alex, L.A.2    Crane, B.R.3    Simon, M.I.4
  • 5
    • 63049110964 scopus 로고    scopus 로고
    • The Rcs two-component system regulates expression of lysozyme inhibitors and is induced by exposure to lysozyme
    • L. Callewaert, K.G. Vanoirbeek, I. Lurquin, C.W. Michiels, and A. Aertsen The Rcs two-component system regulates expression of lysozyme inhibitors and is induced by exposure to lysozyme J. Bacteriol. 191 2009 1979 1981
    • (2009) J. Bacteriol. , vol.191 , pp. 1979-1981
    • Callewaert, L.1    Vanoirbeek, K.G.2    Lurquin, I.3    Michiels, C.W.4    Aertsen, A.5
  • 6
    • 33744993896 scopus 로고    scopus 로고
    • RcsF is an outer membrane lipoprotein involved in the RcsCDB phosphorelay signaling pathway in Escherichia coli
    • DOI 10.1128/JB.00004-06
    • M.P. Castanie-Cornet, K. Cam, and A. Jacq RcsF is an outer membrane lipoprotein involved in the RcsCDB phosphorelay signaling pathway in Escherichia coli J. Bacteriol. 188 2006 4264 4270 (Pubitemid 43865746)
    • (2006) Journal of Bacteriology , vol.188 , Issue.12 , pp. 4264-4270
    • Castanie-Cornet, M.-P.1    Cam, K.2    Jacq, A.3
  • 7
    • 0035490468 scopus 로고    scopus 로고
    • Characterization of the RcsC → YojN → RcsB phosphorelay signaling pathway involved in capsular synthesis in Escherichia coli
    • DOI 10.1271/bbb.65.2364
    • M.H. Chen, S. Takeda, H. Yamada, Y. Ishii, T. Yamashino, and T. Mizuno Characterization of the RcsC→YojN→RcsB phosphorelay signaling pathway involved in capsular synthesis in Escherichia coli Biosci. Biotechnol. Biochem. 65 2001 2364 2367 (Pubitemid 33617223)
    • (2001) Bioscience, Biotechnology and Biochemistry , vol.65 , Issue.10 , pp. 2364-2367
    • Chen, M.H.1    Takeda, S.-I.2    Yamada, H.3    Ishii, Y.4    Yamashino, T.5    Mizuno, T.6
  • 8
    • 0036154798 scopus 로고    scopus 로고
    • Genetic analysis of the RcsC sensor kinase from Escherichia coli K-12
    • DOI 10.1128/jb.184.4.1204-1208.2002
    • D.J. Clarke, S.A. Joyce, C.M. Toutain, A. Jacq, and I.B. Holland Genetic analysis of the RcsC sensor kinase from Escherichia coli K-12 J. Bacteriol. 184 2002 1204 1208 (Pubitemid 34113392)
    • (2002) Journal of Bacteriology , vol.184 , Issue.4 , pp. 1204-1208
    • Clarke, D.J.1    Joyce, S.A.2    Toutain, C.M.3    Jacq, A.4    Holland, I.B.5
  • 9
    • 77955391393 scopus 로고    scopus 로고
    • The HADDOCK web server for data-driven biomolecular docking
    • S.J. de Vries, M. van Dijik, and A.M. Bonvin The HADDOCK web server for data-driven biomolecular docking Nat. Protoc. 5 2010 883 897
    • (2010) Nat. Protoc. , vol.5 , pp. 883-897
    • De Vries, S.J.1    Van Dijik, M.2    Bonvin, A.M.3
  • 10
    • 0032730205 scopus 로고    scopus 로고
    • Histidine kinases: Diversity of domain organization
    • R. Dutta, L. Qin, and M. Inouye Histidine kinases: diversity of domain organization Mol. Microbiol. 34 1999 633 640
    • (1999) Mol. Microbiol. , vol.34 , pp. 633-640
    • Dutta, R.1    Qin, L.2    Inouye, M.3
  • 11
    • 0031089715 scopus 로고    scopus 로고
    • Signal transduction via the histidyl-aspartyl phosphorelay
    • L.A. Egger, H. Park, and M. Inouye Signal transduction via the histidyl-aspartyl phosphorelay Genes Cells 2 1997 167 184 (Pubitemid 127688567)
    • (1997) Genes to Cells , vol.2 , Issue.3 , pp. 167-184
    • Egger, L.A.1    Park, H.2    Inouye, M.3
  • 13
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • DOI 10.1002/elps.1150181505
    • N. Guex, and M.C. Peitsch SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling Electrophoresis 18 1997 2714 2723 (Pubitemid 28059943)
    • (1997) Electrophoresis , vol.18 , Issue.15 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 14
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • DOI 10.1006/jmbi.1997.1284
    • P. Guntert, C. Mumenthaler, and K. Wuthrich Torsion angle dynamics for NMR structure calculation with the new program DYANA J. Mol. Biol. 273 1997 283 298 (Pubitemid 27460230)
    • (1997) Journal of Molecular Biology , vol.273 , Issue.1 , pp. 283-298
    • Guntert, P.1    Mumenthaler, C.2    Wuthrich, K.3
  • 15
    • 0141727625 scopus 로고    scopus 로고
    • Genome-wide analyses revealing a signaling network of the RcsC-YojN-RcsB phosphorelay system in Escherichia coli
    • DOI 10.1128/JB.185.19.5735-5746.2003
    • D. Hagiwara, M. Sugiura, T. Oshima, H. Mori, H. Aiba, T. Yamashino, and T. Mizuno Genome-wide analyses revealing a signaling network of the RcsC-YojN-RcsB phosphorelay system in Escherichia coli J. Bacteriol. 185 2003 5735 5746 (Pubitemid 37176485)
    • (2003) Journal of Bacteriology , vol.185 , Issue.19 , pp. 5735-5746
    • Hagiwara, D.1    Sugiura, M.2    Oshima, T.3    Mori, H.4    Aiba, H.5    Yamashino, T.6    Mizuno, T.7
  • 16
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • DOI 10.1016/S0022-2836(02)00241-3
    • T. Herrmann, P. Guntert, and K. Wuthrich ProteinNMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA J. Mol. Biol. 319 2002 209 227 (Pubitemid 34729497)
    • (2002) Journal of Molecular Biology , vol.319 , Issue.1 , pp. 209-227
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 17
    • 0027428746 scopus 로고
    • Phosphorylation/dephosphorylation of the receiver module at the conserved aspartate residue controls transphosphorylation activity of histidine kinase in sensor protein ArcB of Escherichia coli
    • S. Iuchi Phosphorylation/dephosphorylation of the receiver module at the conserved aspartate residue controls transphosphorylation activity of histidine kinase in sensor protein ArcB of Escherichia coli J. Biol. Chem. 268 1993 23972 23980 (Pubitemid 23335374)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.32 , pp. 23972-23980
    • Iuchi, S.1
  • 18
    • 0026806583 scopus 로고
    • Purification and phosphorylation of the Arc regulatory components of Escherichia coli
    • S. Iuchi, and E.C. Lin Purification and phosphorylation of the Arc regulatory components of Escherichia coli J. Bacteriol. 174 1992 5617 5623
    • (1992) J. Bacteriol. , vol.174 , pp. 5617-5623
    • Iuchi, S.1    Lin, E.C.2
  • 19
    • 0025775119 scopus 로고
    • Modular structure of FixJ: Homology of the transcriptional activator domain with the -35 binding domain of sigma factors
    • D. Kahn, and G. Ditta Modular structure of FixJ: homology of the transcriptional activator domain with the -35 binding domain of sigma factors Mol. Microbiol. 5 1991 987 997 (Pubitemid 21896124)
    • (1991) Molecular Microbiology , vol.5 , Issue.4 , pp. 987-997
    • Kahn, D.1    Ditta, G.2
  • 20
    • 0030686558 scopus 로고    scopus 로고
    • Interaction of the regulator proteins RcsA and RcsB with the promoter of the operon for amylovoran biosynthesis in Erwinia amylovora
    • O. Kelm, C. Kiecker, K. Geider, and F. Bernhard Interaction of the regulator proteins RcsA and RcsB with the promoter of the operon for amylovoran biosynthesis in Erwinia amylovora Mol. Gen. Genet. 256 1997 72 83
    • (1997) Mol. Gen. Genet. , vol.256 , pp. 72-83
    • Kelm, O.1    Kiecker, C.2    Geider, K.3    Bernhard, F.4
  • 21
    • 12744271881 scopus 로고    scopus 로고
    • Structural characterization of Escherichia coli sensor histidine kinase EnvZ: The periplasmic C-terminal core domain is critical for homodimerization
    • A. Khorchid, M. Inouye, and M. Ikura Structural characterization of Escherichia coli sensor histidine kinase EnvZ: the periplasmic C-terminal core domain is critical for homodimerization Biochem. J. 385 2005 255 264
    • (2005) Biochem. J. , vol.385 , pp. 255-264
    • Khorchid, A.1    Inouye, M.2    Ikura, M.3
  • 24
    • 40449091818 scopus 로고    scopus 로고
    • The Rcs phosphorelay is a cell envelope stress response activated by peptidoglycan stress and contributes to intrinsic antibiotic resistance
    • DOI 10.1128/JB.01740-07
    • M.E. Laubacher, and S.E. Ades The Rcs phosphorelay is a cell envelope stress response activated by peptidoglycan stress and contributes to intrinsic antibiotic resistance J. Bacteriol. 190 2008 2065 2074 (Pubitemid 351355330)
    • (2008) Journal of Bacteriology , vol.190 , Issue.6 , pp. 2065-2074
    • Laubacher, M.E.1    Ades, S.E.2
  • 25
    • 0033580642 scopus 로고    scopus 로고
    • Mechanism of CheA protein kinase activation in receptor signaling complexes
    • M.N. Levit, Y. Liu, and J.B. Stock Mechanism of CheA protein kinase activation in receptor signaling complexes Biochemistry 38 1999 6651 6658
    • (1999) Biochemistry , vol.38 , pp. 6651-6658
    • Levit, M.N.1    Liu, Y.2    Stock, J.B.3
  • 27
    • 25144451503 scopus 로고    scopus 로고
    • The Rcs phosphorelay: A complex signal transduction system
    • DOI 10.1146/annurev.micro.59.050405.101230
    • N. Majdalani, and S. Gottesman The Rcs phosphorelay: a complex signal transduction system Annu. Rev. Microbiol. 59 2005 379 405 (Pubitemid 41507437)
    • (2005) Annual Review of Microbiology , vol.59 , pp. 379-405
    • Majdalani, N.1    Gottesman, S.2
  • 28
    • 25144458390 scopus 로고    scopus 로고
    • Role of RcsF in signaling to the Rcs phosphorelay pathway in Escherichia coli
    • DOI 10.1128/JB.187.19.6770-6778.2005
    • N. Majdalani, M. Heck, V. Stout, and S. Gottesman Role of RcsF in signaling to the Rcs phosphorelay pathway in Escherichia coli J. Bacteriol. 187 2005 6770 6778 (Pubitemid 41356251)
    • (2005) Journal of Bacteriology , vol.187 , Issue.19 , pp. 6770-6778
    • Majdalani, N.1    Heck, M.2    Stout, V.3    Gottesman, S.4
  • 29
    • 27644557269 scopus 로고    scopus 로고
    • Primary and secondary modes of DNA recognition by the NarL two-component response regulator
    • DOI 10.1021/bi050734u
    • A.E. Maris, M. Kaczor-Grzeskowiak, Z. Ma, M.L. Kopka, R.P. Gunsalus, and R.E. Dickerson Primary and secondary modes of DNA recognition by the NarL two-component response regulator Biochemistry 44 2005 14538 14552 (Pubitemid 41567462)
    • (2005) Biochemistry , vol.44 , Issue.44 , pp. 14538-14552
    • Maris, A.E.1    Kaczor-Grzeskowiak, M.2    Ma, Z.3    Kopka, M.L.4    Gunsalus, R.P.5    Dickerson, R.E.6
  • 30
    • 0029931125 scopus 로고    scopus 로고
    • Structure and dynamics of a CheY-binding domain of the chemotaxis kinase CheA determined by nuclear magnetic resonance spectroscopy
    • DOI 10.1021/bi952707h
    • M.M. McEvoy, D.R. Muhandiram, L.E. Kay, and F.W. Dalquist Structure and dynamics of a CheY-binding domain of the chemotaxis kinase CheA determined by nuclear magnetic resonance spectroscopy Biochemistry 35 1996 5633 5640 (Pubitemid 26143658)
    • (1996) Biochemistry , vol.35 , Issue.18 , pp. 5633-5640
    • McEvoy, M.M.1    Muhandiram, D.R.2    Kay, L.E.3    Dahlquist, F.W.4
  • 32
    • 0034923123 scopus 로고    scopus 로고
    • Automatic determination of protein backbone resonance assignments from triple resonance nuclear magnetic resonance data
    • DOI 10.1016/S0076-6879(01)39311-4
    • H.N. Moseley, D. Monleon, and G.T. Montelione Automatic determination of protein backbone resonance assignments from triple resonance nuclear magnetic resonance data Methods Enzymol. 339 2001 91 108 (Pubitemid 32666558)
    • (2001) Methods in Enzymology , vol.339 , pp. 91-108
    • Moseley, H.N.B.1    Monleon, D.2    Montelione, G.T.3
  • 33
    • 0035903179 scopus 로고    scopus 로고
    • Crystal structure of the CheA histidine phosphotransfer domain that mediates response regulator phosphorylation in bacterial chemotaxis
    • L. Mourey, S. Da Re, J.D. Pedelacq, T. Tolstykh, C. Faurie, V. Guillet, J.B. Stock, and J.P. Samama Crystal structure of the CheA histidine phosphotransfer domain that mediates response regulator phosphorylation in bacterial chemotaxis J. Biol. Chem. 276 2001 31074 31082
    • (2001) J. Biol. Chem. , vol.276 , pp. 31074-31082
    • Mourey, L.1    Da Re, S.2    Pedelacq, J.D.3    Tolstykh, T.4    Faurie, C.5    Guillet, V.6    Stock, J.B.7    Samama, J.P.8
  • 34
    • 0011559747 scopus 로고
    • Two-component regulatory systems responsive to environmental stimuli share strongly conserved domains with the nitrogen assimilation regulatory genes ntrB and ntrC
    • DOI 10.1073/pnas.83.20.7850
    • B.T. Nixon, C.W. Ronson, and F.M. Ausubel Two-component regulatory systems responsive to environmental stimuli share strongly conserved domains with the nitrogen assimilation regulatory genes ntrB and ntrC Proc. Natl. Acad. Sci. USA 83 1986 7850 7854 (Pubitemid 17183940)
    • (1986) Proceedings of the National Academy of Sciences of the United States of America , vol.83 , Issue.20 , pp. 7850-7854
    • Nixon, B.T.1    Ronson, C.W.2    Ausubel, F.M.3
  • 35
    • 0037705334 scopus 로고    scopus 로고
    • Structural analysis of the DNA-binding domain of the Erwinia amylovora RcsB protein and its interaction with the RcsAB box
    • DOI 10.1074/jbc.M301328200
    • P. Pristovsek, K. Sengupta, F. Löhr, B. Schäfer, M.W. von Trebra, H. Rüterjans, and F. Bernhard Structural analysis of the DNA-binding domain of the Erwinia amylovora RcsB protein and its interaction with the RcsAB box J. Biol. Chem. 278 2003 17752 17759 (Pubitemid 36799378)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.20 , pp. 17752-17759
    • Pristovsek, P.1    Sengupta, K.2    Lohr, F.3    Schafer, B.4    Von Trebra, M.W.5    Ruterjans, H.6    Bernhard, F.7
  • 36
    • 0344875222 scopus 로고    scopus 로고
    • Fast Mapping of Protein-Protein Interfaces by NMR Spectroscopy
    • DOI 10.1021/ja037640x
    • M.L. Reese, and V. Dotsch Fast mapping of protein-protein interfaces by NMR spectroscopy J. Am. Chem. Soc. 125 2003 14250 14251 (Pubitemid 37452344)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.47 , pp. 14250-14251
    • Reese, M.L.1    Dotsch, V.2
  • 37
    • 0033887436 scopus 로고    scopus 로고
    • A tale of two components: A novel kinase and a regulatory switch
    • DOI 10.1038/77915
    • V.L. Robinson, D.R. Buckler, and A.M. Stock A tale of two components: a novel kinase and a regulatory switch Nat. Struct. Biol. 7 2000 626 633 (Pubitemid 30636671)
    • (2000) Nature Structural Biology , vol.7 , Issue.8 , pp. 626-633
    • Robinson, V.L.1    Buckler, D.R.2    Stock, A.M.3
  • 38
    • 5144231590 scopus 로고    scopus 로고
    • Solution structure of the Escherichia coli YojN histidine- phosphotransferase domain and its interaction with cognate phosphoryl receiver domains
    • DOI 10.1016/j.jmb.2004.08.096, PII S0022283604011076
    • V.V. Rogov, F. Bernhard, F. Lohr, and V. Dotsch Solution structure of the Escherichia coli YojN histidine-phosphotransferase domain and its interaction with cognate phosphoryl receiver domains J. Mol. Biol. 343 2004 1035 1048 (Pubitemid 39345962)
    • (2004) Journal of Molecular Biology , vol.343 , Issue.4 , pp. 1035-1048
    • Rogov, V.V.1    Bernhard, F.2    Lohr, F.3    Dotsch, V.4
  • 39
    • 33750336664 scopus 로고    scopus 로고
    • A New Structural Domain in the Escherichia coli RcsC Hybrid Sensor Kinase Connects Histidine Kinase and Phosphoreceiver Domains
    • DOI 10.1016/j.jmb.2006.07.052, PII S0022283606009302
    • V.V. Rogov, N.Y. Rogova, F. Bernhard, A. Koglin, F. Lohr, and V. Dotsch A new structural domain in the Escherichia coli RcsC hybrid sensor kinase connects histidine kinase and phosphoreceiver domains J. Mol. Biol. 364 2006 68 79 (Pubitemid 44634525)
    • (2006) Journal of Molecular Biology , vol.364 , Issue.1 , pp. 68-79
    • Rogov, V.V.1    Rogova, N.Yu.2    Bernhard, F.3    Koglin, A.4    Lohr, F.5    Dotsch, V.6
  • 40
    • 34249109172 scopus 로고    scopus 로고
    • 15N resonances of the truncated Escherichia coli RcsC (700-949), including the phosphoreceiver domain [1]
    • DOI 10.1007/s10858-006-9059-0
    • V.V. Rogov, F. Löhr, N. Rogova, C. Klammt, A. Koglin, F. Bernhard, and V. Dötsch NMR assignment of 1H, 13C and 15N resonances of the truncated Escherichia coli RcsC (700-949), including the phosphoreceiver domain J. Biomol. NMR 38 2007 165 (Pubitemid 46784951)
    • (2007) Journal of Biomolecular NMR , vol.38 , Issue.2 , pp. 165
    • Rogov, V.V.1    Lohr, F.2    Rogova, N.3    Klammt, C.4    Koglin, A.5    Bernhard, F.6    Dotsch, V.7
  • 41
    • 0036427575 scopus 로고    scopus 로고
    • Evolution of signalling in the sporulation phosphorelay
    • DOI 10.1046/j.1365-2958.2002.03186.x
    • K. Stephenson, and J.A. Hoch Evolution of signalling in the sporulation phosphorelay Mol. Microbiol. 46 2002 297 304 (Pubitemid 35345131)
    • (2002) Molecular Microbiology , vol.46 , Issue.2 , pp. 297-304
    • Stephenson, K.1    Hoch, J.A.2
  • 42
    • 0031042699 scopus 로고    scopus 로고
    • Kinetic characterization of phosphotransfer between CheA and CheY in the bacterial chemotaxis signal transduction pathway
    • DOI 10.1021/bi962261k
    • R.C. Stewart Kinetic characterization of phosphotransfer between CheA and CheY in the bacterial chemotaxis signal transduction pathway Biochemistry 36 1997 2030 2040 (Pubitemid 27104693)
    • (1997) Biochemistry , vol.36 , Issue.8 , pp. 2030-2040
    • Stewart, R.C.1
  • 43
    • 1642515778 scopus 로고    scopus 로고
    • Association and Dissociation Kinetics for CheY Interacting with the P2 Domain of CheA
    • DOI 10.1016/j.jmb.2003.11.059
    • R.C. Stewart, and R. Van Bruggen Association and dissociation kinetics for CheY interacting with the P2 domain of CheA J. Mol. Biol. 336 2004 287 301 (Pubitemid 38111177)
    • (2004) Journal of Molecular Biology , vol.336 , Issue.1 , pp. 287-301
    • Stewart, R.C.1    Van Bruggen, R.2
  • 44
    • 0024398149 scopus 로고
    • Protein phosphorylation and regulation of adaptive responses in bacteria
    • J.B. Stock, A.J. Ninfa, and A.M. Stock Protein phosphorylation and regulation of adaptive responses in bacteria Microbiol. Rev. 53 1989 450 490 (Pubitemid 20006368)
    • (1989) Microbiological Reviews , vol.53 , Issue.4 , pp. 450-490
    • Stock, J.B.1    Ninfa, A.J.2    Stock, A.M.3
  • 45
    • 0035033385 scopus 로고    scopus 로고
    • A novel feature of the multistep phosphorelay in Escherichia coli: A revised model of the RcsC → YojN → RcsB signalling pathway implicated in capsular synthesis and swarming behaviour
    • DOI 10.1046/j.1365-2958.2001.02393.x
    • S. Takeda, Y. Fujisawa, M. Matsubara, H. Aiba, and T. Mizuno A novel feature of the multistep phosphorelay in Escherichia coli: a revised model of the RcsC → YojN → RcsB signalling pathway implicated in capsular synthesis and swarming behaviour Mol. Microbiol. 40 2001 440 450 (Pubitemid 32391638)
    • (2001) Molecular Microbiology , vol.40 , Issue.2 , pp. 440-450
    • Takeda, S.-I.1    Fujisawa, Y.2    Matsubara, M.3    Aiba, H.4    Mizuno, T.5
  • 47
    • 0030466066 scopus 로고    scopus 로고
    • Central role of the BvgS receiver as a phosphorylated intermediate in a complex two-component phosphorelay
    • DOI 10.1074/jbc.271.52.33176
    • M.A. Uhl, and J.F. Miller Central role of the BvgS receiver as a phosphorylated intermediate in a complex two-component phosphorelay J. Biol. Chem. 271 1996 33176 33180 (Pubitemid 27010122)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.52 , pp. 33176-33180
    • Uhl, M.A.1    Miller, J.F.2
  • 48
    • 33745471490 scopus 로고    scopus 로고
    • The crystal structure of beryllofluoride Spo0F in complex with the phosphotransferase Spo0B represents a phosphotransfer pretransition state
    • DOI 10.1128/JB.00160-06
    • K.I. Varughese, I. Tsigelny, and H. Zhao The crystal structure of beryllofluoride Spo0F in complex with the phosphotransferase Spo0B represents a phosphotransfer pretransition state J. Bacteriol. 188 2006 4970 4977 (Pubitemid 43956094)
    • (2006) Journal of Bacteriology , vol.188 , Issue.13 , pp. 4970-4977
    • Varughese, K.I.1    Tsigelny, I.2    Zhao, H.3
  • 49
    • 0034629097 scopus 로고    scopus 로고
    • The RcsAB box. Characterization of a new operator essential for the regulation of exopolysaccharide biosynthesis in enteric bacteria
    • DOI 10.1074/jbc.275.10.7013
    • M. Wehland, and F. Bernhard The RcsAB box. Characterization of a new operator essential for the regulation of exopolysaccharide biosynthesis in enteric bacteria J. Biol. Chem. 275 2000 7013 7020 (Pubitemid 30146246)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.10 , pp. 7013-7020
    • Wehland, M.1    Bernhard, F.2
  • 50
    • 0033525083 scopus 로고    scopus 로고
    • Identification of an RcsA/RcsB recognition motif in the promoters of exopolysaccharide biosynthetic operons from Erwinia amylovora and Pantoea stewartii subspecies stewartii
    • DOI 10.1074/jbc.274.6.3300
    • M. Wehland, C. Kiecker, D.L. Coplin, O. Kelm, W. Saenger, and F. Bernhard Identification of an RcsA/RcsB recognition motif in the promotors of exopolysaccharide biosynthetic operons from Erwinia amylovora and Pantoea stewartii subspecies stewartii J. Biol. Chem. 274 1999 3300 3307 (Pubitemid 29077165)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.6 , pp. 3300-3307
    • Wehland, M.1    Kiecker, C.2    Coplin, D.L.3    Kelm, O.4    Saenger, W.5    Bernhard, F.6
  • 51
    • 0035369115 scopus 로고    scopus 로고
    • Histidine kinases and response regulator proteins in two-component signaling systems
    • DOI 10.1016/S0968-0004(01)01852-7, PII S0968000401018527
    • A.H. West, and A.M. Stock Histidine kinases and response regulator proteins in two-component signaling systems Trends Biochem. Sci. 26 2001 369 376 (Pubitemid 32530655)
    • (2001) Trends in Biochemical Sciences , vol.26 , Issue.6 , pp. 369-376
    • West, A.H.1    Stock, A.M.2
  • 53
    • 0344436666 scopus 로고    scopus 로고
    • The Yeast YPD1/SLN1 Complex: Insights into Molecular Recognition in Two-Component Signaling Systems
    • DOI 10.1016/j.str.2003.10.016
    • Q. Xu, S.W. Porter, and A.H. West The yeast YPD1/SLN1 complex: insights into molecular recognition in two-component signaling systems Structure 11 2003 1569 1581 (Pubitemid 37510356)
    • (2003) Structure , vol.11 , Issue.12 , pp. 1569-1581
    • Xu, Q.1    Porter, S.W.2    West, A.H.3
  • 54
    • 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
    • J. Zapf, U. Sen, Madhusudan, J.A. Hoch, and K.I. Varughese 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 2000 851 862
    • (2000) Structure , vol.8 , pp. 851-862
    • Zapf, J.1    Sen, U.2    Madhusudan3    Hoch, J.A.4    Varughese, K.I.5
  • 55
    • 22144475428 scopus 로고    scopus 로고
    • Distribution and evolution of multiple-step phosphorelay in prokaryotes: Lateral domain recruitment involved in the formation of hybrid-type histidine kinases
    • DOI 10.1099/mic.0.27987-0
    • W. Zhang, and L. Shi Distribution and evolution of multiple-step phosphorelay in prokaryotes: lateral domain recruitment involved in the formation of hybrid-type histidine kinases Microbiology 151 2005 2159 2173 (Pubitemid 40984290)
    • (2005) Microbiology , vol.151 , Issue.7 , pp. 2159-2173
    • Zhang, W.1    Shi, L.2
  • 56
    • 37449018128 scopus 로고    scopus 로고
    • Crystal Structure of a Complex between the Phosphorelay Protein YPD1 and the Response Regulator Domain of SLN1 Bound to a Phosphoryl Analog
    • DOI 10.1016/j.jmb.2007.11.045, PII S0022283607015161
    • X. Zhao, D.M. Copeland, A.S. Soares, and A.H. West Crystal structure of a complex between the phosphorelay protein YPD1 and the response regulator domain of SLN1 bound to a phosphoryl analog J. Mol. Biol. 375 2008 1141 1151 (Pubitemid 50012875)
    • (2008) Journal of Molecular Biology , vol.375 , Issue.4 , pp. 1141-1151
    • Zhao, X.1    Copeland, D.M.2    Soares, A.S.3    West, A.H.4
  • 57
    • 0030043573 scopus 로고    scopus 로고
    • Phosphotransfer and CheY-binding domains of the histidine autokinase CheA are joined by a flexible linker
    • DOI 10.1021/bi951960e
    • H. Zhou, M.M. McEvoy, D.F. Lowry, R.V. Swanson, M.I. Simon, and F.W. Dahlquist Phosphotransfer and CheY-binding domains of the histidine autokinase CheA are joined by a flexible linker Biochemistry 35 1996 433 443 (Pubitemid 26033914)
    • (1996) Biochemistry , vol.35 , Issue.2 , pp. 433-443
    • Zhou, H.1    McEvoy, M.M.2    Lowry, D.F.3    Swanson, R.V.4    Simon, M.I.5    Dahlquist, F.W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.