메뉴 건너뛰기




Volumn 6, Issue 5, 2011, Pages

Dissecting the specificity of protein-protein interaction in bacterial two-component signaling: Orphans and crosstalks

Author keywords

[No Author keywords available]

Indexed keywords

ORPHAN NUCLEAR RECEPTOR; AMINO ACID; BACTERIAL PROTEIN; PROTEIN HISTIDINE KINASE; PROTEIN KINASE; PROTEIN-HISTIDINE KINASE;

EID: 79955792165     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0019729     Document Type: Article
Times cited : (83)

References (36)
  • 1
    • 0034035586 scopus 로고    scopus 로고
    • Two-component and phosphorelay signal transduction
    • Hoch JA, (2000) Two-component and phosphorelay signal transduction. Curr Opin Microbiol 3: 165-170.
    • (2000) Curr Opin Microbiol , vol.3 , pp. 165-170
    • Hoch, J.A.1
  • 2
    • 75549092201 scopus 로고    scopus 로고
    • The MiST2 database: a comprehensive genomics resource on microbial signal transduction
    • Ulrich LE, Zhulin IB, (2009) The MiST2 database: a comprehensive genomics resource on microbial signal transduction. Nucleic Acids Res 38: D401-D407.
    • (2009) Nucleic Acids Res , vol.38
    • Ulrich, L.E.1    Zhulin, I.B.2
  • 3
    • 36549003158 scopus 로고    scopus 로고
    • Sensor complexes regulating two-component signal transduction
    • Szurmant H, White RA, Hoch JA, (2007) Sensor complexes regulating two-component signal transduction. Curr Opin Struct Biol 17: 706-715.
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 706-715
    • Szurmant, H.1    White, R.A.2    Hoch, J.A.3
  • 4
    • 44449112421 scopus 로고    scopus 로고
    • Specificity in two-component signal transduction pathways
    • Laub MT, 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
  • 5
    • 77949915674 scopus 로고    scopus 로고
    • Interaction fidelity in two-component signaling
    • Szurmant H, Hoch JA, (2010) Interaction fidelity in two-component signaling. Curr Opin Microbiol 13: 190-197.
    • (2010) Curr Opin Microbiol , vol.13 , pp. 190-197
    • Szurmant, H.1    Hoch, J.A.2
  • 6
    • 0034879819 scopus 로고    scopus 로고
    • Keeping signals straight in phosphorelay signal transduction
    • Hoch JA, Varughese KI, (2001) Keeping signals straight in phosphorelay signal transduction. J Bacteriol 183: 4941-4949.
    • (2001) J Bacteriol , vol.183 , pp. 4941-4949
    • Hoch, J.A.1    Varughese, K.I.2
  • 7
    • 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
  • 8
    • 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    Madhusudan3    Hoch, J.A.4    Varughese, K.I.5
  • 9
    • 12544258487 scopus 로고    scopus 로고
    • Functional characterization in vitro of all two-component signal transduction systems from Escherichia coli
    • Yamamoto K, Hirao K, Oshima T, Aiba H, Utsumi R, et al. (2005) Functional characterization in vitro of all two-component signal transduction systems from Escherichia coli. J Biol Chem 280: 1448-1456.
    • (2005) J Biol Chem , vol.280 , pp. 1448-1456
    • Yamamoto, K.1    Hirao, K.2    Oshima, T.3    Aiba, H.4    Utsumi, R.5
  • 10
    • 38749132556 scopus 로고    scopus 로고
    • Bioinformatics and experimental analysis of proteins of two-component systems in Myxococcus xanthus
    • Shi X, Wegener-Feldbrugge S, Huntley S, Hamann N, Hedderich R, et al. (2008) Bioinformatics and experimental analysis of proteins of two-component systems in Myxococcus xanthus. J Bacteriol 190: 613-624.
    • (2008) J Bacteriol , vol.190 , pp. 613-624
    • Shi, X.1    Wegener-Feldbrugge, S.2    Huntley, S.3    Hamann, N.4    Hedderich, R.5
  • 11
    • 0033711144 scopus 로고    scopus 로고
    • Multiple histidine kinases regulate entry into stationary phase and sporulation in Bacillus subtilis
    • Jiang M, Shao W, Perego M, Hoch JA, (2000) Multiple histidine kinases regulate entry into stationary phase and sporulation in Bacillus subtilis. Mol Microbiol 38: 535-542.
    • (2000) Mol Microbiol , vol.38 , pp. 535-542
    • Jiang, M.1    Shao, W.2    Perego, M.3    Hoch, J.A.4
  • 12
    • 2942584862 scopus 로고    scopus 로고
    • Diversity in chemotaxis mechanisms among the bacteria and archaea
    • Szurmant H, Ordal GW, (2004) Diversity in chemotaxis mechanisms among the bacteria and archaea. Microbiol Mol Biol Rev 68: 301-319.
    • (2004) Microbiol Mol Biol Rev , vol.68 , pp. 301-319
    • Szurmant, H.1    Ordal, G.W.2
  • 13
    • 33645050137 scopus 로고    scopus 로고
    • Interactions between the YycFG and PhoPR two-component systems in Bacillus subtilis: the PhoR kinase phosphorylates the non-cognate YycF response regulator upon phosphate limitation
    • Howell A, Dubrac S, Noone D, Varughese KI, Devine K, (2006) Interactions between the YycFG and PhoPR two-component systems in Bacillus subtilis: the PhoR kinase phosphorylates the non-cognate YycF response regulator upon phosphate limitation. Mol Microbiol 59: 1199-1215.
    • (2006) Mol Microbiol , vol.59 , pp. 1199-1215
    • Howell, A.1    Dubrac, S.2    Noone, D.3    Varughese, K.I.4    Devine, K.5
  • 14
    • 41749088673 scopus 로고    scopus 로고
    • Bacitracin sensing in Bacillus subtilis
    • Rietkotter E, Hoyer D, Mascher T, (2008) Bacitracin sensing in Bacillus subtilis. Mol Microbiol 68: 768-785.
    • (2008) Mol Microbiol , vol.68 , pp. 768-785
    • Rietkotter, E.1    Hoyer, D.2    Mascher, T.3
  • 15
    • 77949916106 scopus 로고    scopus 로고
    • Inference of direct residue contacts in two-component signaling
    • Lunt B, Szurmant H, Procaccini A, Hoch JA, Hwa T, et al. (2010) Inference of direct residue contacts in two-component signaling. Methods Enzymol 471: 17-41.
    • (2010) Methods Enzymol , vol.471 , pp. 17-41
    • Lunt, B.1    Szurmant, H.2    Procaccini, A.3    Hoch, J.A.4    Hwa, T.5
  • 16
    • 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
  • 17
    • 70149115237 scopus 로고    scopus 로고
    • Constraint satisfaction problems and neural networks: A statistical physics perspective
    • Mezard M, Mora T, (2009) Constraint satisfaction problems and neural networks: A statistical physics perspective. J Physiol Paris 103: 107-113.
    • (2009) J Physiol Paris , vol.103 , pp. 107-113
    • Mezard, M.1    Mora, T.2
  • 19
    • 76749112068 scopus 로고    scopus 로고
    • Disentangling direct from indirect co-evolution of residues in protein alignments
    • Burger L, van Nimwegen E, (2010) Disentangling direct from indirect co-evolution of residues in protein alignments. PLoS Comput Biol 6: e1000633.
    • (2010) PLoS Comput Biol , vol.6
    • Burger, L.1    van Nimwegen, E.2
  • 20
    • 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
  • 21
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley WC, White SH, (1996) Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat Struct Biol 3: 842-848.
    • (1996) Nat Struct Biol , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 22
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J, Doolittle RF, (1982) A simple method for displaying the hydropathic character of a protein. J Mol Biol 157: 105-132.
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 24
    • 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
  • 25
    • 26444481955 scopus 로고    scopus 로고
    • Two-component signal transduction pathways regulating growth and cell cycle progression in a bacterium: a system-level analysis
    • Skerker JM, Prasol MS, Perchuk BS, Biondi EG, Laub MT, (2005) Two-component signal transduction pathways regulating growth and cell cycle progression in a bacterium: a system-level analysis. PLoS Biol 3: e334.
    • (2005) PLoS Biol , vol.3
    • Skerker, J.M.1    Prasol, M.S.2    Perchuk, B.S.3    Biondi, E.G.4    Laub, M.T.5
  • 26
    • 10344238965 scopus 로고    scopus 로고
    • Structural basis of activity and allosteric control of diguanylate cyclase
    • Chan C, Paul R, Samoray D, Amiot NC, Giese B, et al. (2004) Structural basis of activity and allosteric control of diguanylate cyclase. Proc Natl Acad Sci U S A 101: 17084-17089.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 17084-17089
    • Chan, C.1    Paul, R.2    Samoray, D.3    Amiot, N.C.4    Giese, B.5
  • 27
    • 0037346498 scopus 로고    scopus 로고
    • Role of the GGDEF regulator PleD in polar development of Caulobacter crescentus
    • Aldridge P, Paul R, Goymer P, Rainey P, Jenal U, (2003) Role of the GGDEF regulator PleD in polar development of Caulobacter crescentus. Mol Microbiol 47: 1695-1708.
    • (2003) Mol Microbiol , vol.47 , pp. 1695-1708
    • Aldridge, P.1    Paul, R.2    Goymer, P.3    Rainey, P.4    Jenal, U.5
  • 28
    • 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
  • 29
    • 0033539643 scopus 로고    scopus 로고
    • A novel bacterial tyrosine kinase essential for cell division and differentiation
    • Wu J, 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.1    Ohta, N.2    Zhao, J.L.3    Newton, A.4
  • 30
    • 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
  • 31
    • 0033852729 scopus 로고    scopus 로고
    • The CitST two-component system regulates the expression of the Mg-citrate transporter in Bacillus subtilis
    • Yamamoto H, Murata M, Sekiguchi J, (2000) The CitST two-component system regulates the expression of the Mg-citrate transporter in Bacillus subtilis. Mol Microbiol 37: 898-912.
    • (2000) Mol Microbiol , vol.37 , pp. 898-912
    • Yamamoto, H.1    Murata, M.2    Sekiguchi, J.3
  • 32
    • 0141703516 scopus 로고    scopus 로고
    • The Bacillus subtilis ywkA gene encodes a malic enzyme and its transcription is activated by the YufL/YufM two-component system in response to malate
    • Doan T, Servant P, Tojo S, Yamaguchi H, Lerondel G, et al. (2003) The Bacillus subtilis ywkA gene encodes a malic enzyme and its transcription is activated by the YufL/YufM two-component system in response to malate. Microbiology 149: 2331-2343.
    • (2003) Microbiology , vol.149 , pp. 2331-2343
    • Doan, T.1    Servant, P.2    Tojo, S.3    Yamaguchi, H.4    Lerondel, G.5
  • 33
    • 16244398023 scopus 로고    scopus 로고
    • Transcriptional response of Escherichia coli to external copper
    • Yamamoto K, Ishihama A, (2005) Transcriptional response of Escherichia coli to external copper. Mol Microbiol 56: 215-227.
    • (2005) Mol Microbiol , vol.56 , pp. 215-227
    • Yamamoto, K.1    Ishihama, A.2
  • 34
    • 39149114704 scopus 로고    scopus 로고
    • Accurate prediction of protein-protein interactions from sequence alignments using a Bayesian method
    • Burger L, van Nimwegen E, (2008) Accurate prediction of protein-protein interactions from sequence alignments using a Bayesian method. Mol Syst Biol 4: 165.
    • (2008) Mol Syst Biol , vol.4 , pp. 165
    • Burger, L.1    van Nimwegen, E.2
  • 35
    • 0031743421 scopus 로고    scopus 로고
    • Profile hidden Markov models
    • Eddy SR, (1998) Profile hidden Markov models. Bioinformatics 14: 755-763.
    • (1998) Bioinformatics , vol.14 , pp. 755-763
    • Eddy, S.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.