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Volumn 422, Issue , 2007, Pages 75-101

Features of Protein-Protein Interactions in Two-Component Signaling Deduced from Genomic Libraries

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHOTRANSFERASE;

EID: 34447104524     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(06)22004-4     Document Type: Chapter
Times cited : (46)

References (49)
  • 1
    • 0023660022 scopus 로고
    • Correlation of co-ordinated amino acid substitutions with function in viruses related to tobacco mosaic virus
    • Altschuh D., Lesk A.M., Bloomer A.C., and Klug A. Correlation of co-ordinated amino acid substitutions with function in viruses related to tobacco mosaic virus. J. Mol. Biol. 193 (1987) 693-707
    • (1987) J. Mol. Biol. , vol.193 , pp. 693-707
    • Altschuh, D.1    Lesk, A.M.2    Bloomer, A.C.3    Klug, A.4
  • 3
    • 0033977832 scopus 로고    scopus 로고
    • Correlations among amino acid sites in bHLH protein domains: An information theoretic analysis
    • Atchley W.R., Wollenberg K.R., Fitch W.M., Terhalle W., and Dress A.W. Correlations among amino acid sites in bHLH protein domains: An information theoretic analysis. Mol. Biol. Evol. 17 (2000) 164-178
    • (2000) Mol. Biol. Evol. , vol.17 , pp. 164-178
    • Atchley, W.R.1    Wollenberg, K.R.2    Fitch, W.M.3    Terhalle, W.4    Dress, A.W.5
  • 5
    • 0141941680 scopus 로고    scopus 로고
    • Making informed decisions: Regulatory interactions between two-component systems
    • Bijlsma J.J., and Groisman E.A. Making informed decisions: Regulatory interactions between two-component systems. Trends Microbiol. 11 (2003) 359-366
    • (2003) Trends Microbiol. , vol.11 , pp. 359-366
    • Bijlsma, J.J.1    Groisman, E.A.2
  • 6
    • 0346733329 scopus 로고    scopus 로고
    • Are protein-protein interfaces more conserved in sequence than the rest of the protein surface?
    • Caffrey D.R., Somaroo S., Hughes J.D., Mintseris J., and Huang E.S. Are protein-protein interfaces more conserved in sequence than the rest of the protein surface?. Protein Sci. 13 (2004) 190-202
    • (2004) Protein Sci. , vol.13 , pp. 190-202
    • Caffrey, D.R.1    Somaroo, S.2    Hughes, J.D.3    Mintseris, J.4    Huang, E.S.5
  • 7
    • 0028832687 scopus 로고
    • Covariation of residues in the homeodomain sequence family
    • Clarke N.D. Covariation of residues in the homeodomain sequence family. Protein Sci. 4 (1995) 2269-2278
    • (1995) Protein Sci. , vol.4 , pp. 2269-2278
    • Clarke, N.D.1
  • 9
    • 0031743421 scopus 로고    scopus 로고
    • Profile hidden Markov models
    • Eddy S.R. Profile hidden Markov models. Bioinformatics 14 (1998) 755-763
    • (1998) Bioinformatics , vol.14 , pp. 755-763
    • Eddy, S.R.1
  • 10
    • 13244255415 scopus 로고    scopus 로고
    • MUSCLE: A multiple sequence alignment method with reduced time and space complexity
    • Edgar R. MUSCLE: A multiple sequence alignment method with reduced time and space complexity. BMC Bioinformatics 5 (2004) 113
    • (2004) BMC Bioinformatics , vol.5 , pp. 113
    • Edgar, R.1
  • 11
    • 0033523989 scopus 로고    scopus 로고
    • Protein interaction maps for complete genomes based on gene fusion events
    • Enright A.J., Iliopoulos I., Kyrpides N.C., and Ouzounis C.A. Protein interaction maps for complete genomes based on gene fusion events. Nature 402 (1999) 86-90
    • (1999) Nature , vol.402 , pp. 86-90
    • Enright, A.J.1    Iliopoulos, I.2    Kyrpides, N.C.3    Ouzounis, C.A.4
  • 12
    • 3042842115 scopus 로고    scopus 로고
    • Influence of conservation on calculations of amino acid covariance in multiple sequence alignments
    • Fodor A.A., and Aldrich R.W. Influence of conservation on calculations of amino acid covariance in multiple sequence alignments. Proteins Structure Function Bioinformatics 56 (2004) 211-221
    • (2004) Proteins Structure Function Bioinformatics , vol.56 , pp. 211-221
    • Fodor, A.A.1    Aldrich, R.W.2
  • 15
    • 0033277340 scopus 로고    scopus 로고
    • The histidine protein kinase superfamily
    • Grebe T.W., and Stock J.B. The histidine protein kinase superfamily. Adv. Microb. Physiol. 41 (1999) 139-227
    • (1999) Adv. Microb. Physiol. , vol.41 , pp. 139-227
    • Grebe, T.W.1    Stock, J.B.2
  • 16
    • 0034035586 scopus 로고    scopus 로고
    • Two-component and phosphorelay signal transduction
    • Hoch J.A. Two-component and phosphorelay signal transduction. Curr. Opin. Microbiol. 3 (2000) 165-170
    • (2000) Curr. Opin. Microbiol. , vol.3 , pp. 165-170
    • Hoch, J.A.1
  • 17
    • 33645299313 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 K.I., and Devine K. 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. 60 (2006) 535
    • (2006) Mol. Microbiol. , vol.60 , pp. 535
    • Howell, A.1    Dubrac, S.2    Noone, D.3    Varughese, K.I.4    Devine, K.5
  • 18
    • 0030921594 scopus 로고    scopus 로고
    • A database for post-genome analysis
    • Kanehisa M. A database for post-genome analysis. Trends Genet. 13 (1997) 375-376
    • (1997) Trends Genet. , vol.13 , pp. 375-376
    • Kanehisa, M.1
  • 20
    • 0036721218 scopus 로고    scopus 로고
    • Mapping pathways of allosteric communication in GroEL by analysis of correlated mutations
    • Kass I., and Horovitz A. Mapping pathways of allosteric communication in GroEL by analysis of correlated mutations. Proteins Struct. Funct. Genet. 48 (2002) 611-617
    • (2002) Proteins Struct. Funct. Genet. , vol.48 , pp. 611-617
    • Kass, I.1    Horovitz, A.2
  • 21
    • 13744252890 scopus 로고    scopus 로고
    • MAFFT version 5: Improvement in accuracy of multiple sequence alignment
    • Katoh K., Kuma K.-i., Toh H., and Miyata T. MAFFT version 5: Improvement in accuracy of multiple sequence alignment. Nucleic Acids Res. 33 (2005) 511-518
    • (2005) Nucleic Acids Res. , vol.33 , pp. 511-518
    • Katoh, K.1    Kuma, K.-i.2    Toh, H.3    Miyata, T.4
  • 23
    • 0000702165 scopus 로고
    • Mutual information functions versus correlation functions
    • Li W. Mutual information functions versus correlation functions. J. Stat. Phys. V60 (1990) 823-837
    • (1990) J. Stat. Phys. , vol.V60 , pp. 823-837
    • Li, W.1
  • 24
  • 25
    • 0033536602 scopus 로고    scopus 로고
    • Evolutionarily conserved pathways of energetic connectivity in protein families
    • Lockless S.W., and Ranganathan R. Evolutionarily conserved pathways of energetic connectivity in protein families. Science 286 (1999) 295-299
    • (1999) Science , vol.286 , pp. 295-299
    • Lockless, S.W.1    Ranganathan, R.2
  • 26
    • 25144458390 scopus 로고    scopus 로고
    • Role of RcsF in signaling to the Rcs phosphorelay pathway in Escherichia coli
    • Majdalani N., Heck M., Stout V., and Gottesman S. Role of RcsF in signaling to the Rcs phosphorelay pathway in Escherichia coli. J. Bacteriol. 187 (2005) 6770-6778
    • (2005) J. Bacteriol. , vol.187 , pp. 6770-6778
    • Majdalani, N.1    Heck, M.2    Stout, V.3    Gottesman, S.4
  • 27
    • 0033618555 scopus 로고    scopus 로고
    • Detecting protein function and protein-protein interactions from genome sequences
    • Marcotte E.M., Pellegrini M., Ng H.-L., Rice D.W., Yeates T.O., and Eisenberg D. Detecting protein function and protein-protein interactions from genome sequences. Science 285 (1999) 751-753
    • (1999) Science , vol.285 , pp. 751-753
    • Marcotte, E.M.1    Pellegrini, M.2    Ng, H.-L.3    Rice, D.W.4    Yeates, T.O.5    Eisenberg, D.6
  • 28
    • 29244433095 scopus 로고    scopus 로고
    • Structure of the entire cytoplasmic portion of a sensor histidine-kinase protein
    • Marina A., Waldburger C.D., and Hendrickson W.A. Structure of the entire cytoplasmic portion of a sensor histidine-kinase protein. EMBO J. 24 (2005) 4247-4259
    • (2005) EMBO J. , vol.24 , pp. 4247-4259
    • Marina, A.1    Waldburger, C.D.2    Hendrickson, W.A.3
  • 29
    • 0024061466 scopus 로고
    • Crosstalk between bacterial chemotaxis signal transduction proteins and regulators of transcription of the Ntr regulon: Evidence that nitrogen assimilation and chemotaxis are controlled by a common phosphotransfer mechanism
    • Ninfa A.J., Ninfa E.G., Lupas A.N., Stock A., Magasanik B., and Stock J. Crosstalk between bacterial chemotaxis signal transduction proteins and regulators of transcription of the Ntr regulon: Evidence that nitrogen assimilation and chemotaxis are controlled by a common phosphotransfer mechanism. Proc. Natl. Acad. Sci. USA 85 (1988) 5492-5496
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5492-5496
    • Ninfa, A.J.1    Ninfa, E.G.2    Lupas, A.N.3    Stock, A.4    Magasanik, B.5    Stock, J.6
  • 30
    • 0034623005 scopus 로고    scopus 로고
    • T-coffee: A novel method for fast and accurate multiple sequence alignment
    • Notredame C., Higgins D.G., and Heringa J. T-coffee: A novel method for fast and accurate multiple sequence alignment. J. Mol. Biol. 302 (2000) 205-217
    • (2000) J. Mol. Biol. , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 32
    • 0027243652 scopus 로고
    • Signal transduction schemes of bacteria
    • Parkinson J.S. Signal transduction schemes of bacteria. Cell 73 (1993) 857-871
    • (1993) Cell , vol.73 , pp. 857-871
    • Parkinson, J.S.1
  • 33
    • 0030821675 scopus 로고    scopus 로고
    • Correlated mutations contain information about protein-protein interaction
    • Pazos F., Helmer-Citterich M., Ausiello G., and Valencia A. Correlated mutations contain information about protein-protein interaction. J. Mol. Biol. 271 (1997) 511-523
    • (1997) J. Mol. Biol. , vol.271 , pp. 511-523
    • Pazos, F.1    Helmer-Citterich, M.2    Ausiello, G.3    Valencia, A.4
  • 34
    • 0035177259 scopus 로고    scopus 로고
    • Similarity of phylogenetic trees as indicator of protein-protein interaction
    • Pazos F., and Valencia A. Similarity of phylogenetic trees as indicator of protein-protein interaction. Protein Eng. 14 (2001) 609-614
    • (2001) Protein Eng. , vol.14 , pp. 609-614
    • Pazos, F.1    Valencia, A.2
  • 35
    • 0035162594 scopus 로고    scopus 로고
    • RefSeq and LocusLink: NCBI gene-centered resources
    • Pruitt K.D., and Maglott D.R. RefSeq and LocusLink: NCBI gene-centered resources. Nucleic Acids Res. 29 (2001) 137-140
    • (2001) Nucleic Acids Res. , vol.29 , pp. 137-140
    • Pruitt, K.D.1    Maglott, D.R.2
  • 36
    • 0037436412 scopus 로고    scopus 로고
    • Exploiting the co-evolution of interacting proteins to discover interaction specificity
    • Ramani A.K., and Marcotte E.M. Exploiting the co-evolution of interacting proteins to discover interaction specificity. J. Mol. Biol. 327 (2003) 273-284
    • (2003) J. Mol. Biol. , vol.327 , pp. 273-284
    • Ramani, A.K.1    Marcotte, E.M.2
  • 38
    • 26444481955 scopus 로고    scopus 로고
    • Two-component signal transduction pathways regulating growth and cell cycle progression in a bacterium: A system-level analysis
    • Skerker J.M., Prasol M.S., Perchuk B.S., Biondi E.G., and Laub M.T. Two-component signal transduction pathways regulating growth and cell cycle progression in a bacterium: A system-level analysis. PLoS Biol. 3 (2005) 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
  • 39
    • 0041450894 scopus 로고
    • The optimal graph partitioning problem
    • Sören H., and Michael Malmros S. The optimal graph partitioning problem. OR Spectrum V15 (1993) 1-8
    • (1993) OR Spectrum , vol.V15 , pp. 1-8
    • Sören, H.1    Michael Malmros, S.2
  • 41
    • 0024398149 scopus 로고
    • Protein phosphorylation and regulation of adaptive responses in bacteria
    • Stock J.B., Ninfa A.J., and Stock A.M. Protein phosphorylation and regulation of adaptive responses in bacteria. Microbiol. Rev. 53 (1989) 450-490
    • (1989) Microbiol. Rev. , vol.53 , pp. 450-490
    • Stock, J.B.1    Ninfa, A.J.2    Stock, A.M.3
  • 42
    • 0037219686 scopus 로고    scopus 로고
    • Evolutionarily conserved networks of residues mediate allosteric communication in proteins
    • Suel G.M., Lockless S.W., Wall M.A., and Ranganathan R. Evolutionarily conserved networks of residues mediate allosteric communication in proteins. Nat. Struct. Biol. 10 (2003) 59-69
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 59-69
    • Suel, G.M.1    Lockless, S.W.2    Wall, M.A.3    Ranganathan, R.4
  • 43
    • 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
    • Takeda S.-i., Fujisawa Y., Matsubara M., Aiba H., and Mizuno T. 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
    • (2001) Mol. Microbiol. , vol.40 , pp. 440-450
    • Takeda, S.-i.1    Fujisawa, Y.2    Matsubara, M.3    Aiba, H.4    Mizuno, T.5
  • 44
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 45
    • 0036148388 scopus 로고    scopus 로고
    • Investigation of in vivo cross-talk between key two-component systems of Escherichia coli
    • Verhamme D.T., Arents J.C., Postma P.W., Crielaard W., and Hellingwerf K.J. Investigation of in vivo cross-talk between key two-component systems of Escherichia coli. Microbiology 148 (2002) 69-78
    • (2002) Microbiology , vol.148 , pp. 69-78
    • Verhamme, D.T.1    Arents, J.C.2    Postma, P.W.3    Crielaard, W.4    Hellingwerf, K.J.5
  • 48
    • 0021012648 scopus 로고
    • Detailed analysis of the higher-order structure of 16S-like ribosomal ribonucleic acids
    • Woese C.R., Gutell R., Gupta R., and Noller H.F. Detailed analysis of the higher-order structure of 16S-like ribosomal ribonucleic acids. Microbiol. Mol. Biol. Rev. 47 (1983) 621-669
    • (1983) Microbiol. Mol. Biol. Rev. , vol.47 , pp. 621-669
    • Woese, C.R.1    Gutell, R.2    Gupta, R.3    Noller, H.F.4
  • 49
    • 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., and Varughese K.I. 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    Madhusudan Hoch, J.A.3    Varughese, K.I.4


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