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Volumn 185, Issue 2, 2003, Pages 544-552

Different evolutionary constraints on chemotaxis proteins CheW and CheY revealed by heterologous expression studies and protein sequence analysis

Author keywords

[No Author keywords available]

Indexed keywords

CHEW PROTEIN; PROTEIN; PROTEIN CHEY; UNCLASSIFIED DRUG;

EID: 0037224551     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.2.544-552.2003     Document Type: Article
Times cited : (28)

References (46)
  • 1
    • 0023777735 scopus 로고
    • Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli
    • Amann, E., B. Ochs, and K. J. Abel. 1988. Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli. Gene 69:301-315.
    • (1988) Gene , vol.69 , pp. 301-315
    • Amann, E.1    Ochs, B.2    Abel, K.J.3
  • 2
    • 0029790352 scopus 로고    scopus 로고
    • Behavioral responses of Escherichia coli to changes in redox potential
    • Bespalov, V. A., I. B. Zhulin, and B. L. Taylor. 1996. Behavioral responses of Escherichia coli to changes in redox potential. Proc. Natl. Acad. Sci. USA 93:10084-10089.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10084-10089
    • Bespalov, V.A.1    Zhulin, I.B.2    Taylor, B.L.3
  • 3
    • 0033534368 scopus 로고    scopus 로고
    • Structure of CheA, a signal-transducing histidine kinase
    • Bilwes, A. M., L. A. Alex, B. R. Crane, and M. I. Simon. 1999. Structure of CheA, a signal-transducing histidine kinase. Cell 96:131-141.
    • (1999) Cell , vol.96 , pp. 131-141
    • Bilwes, A.M.1    Alex, L.A.2    Crane, B.R.3    Simon, M.I.4
  • 4
    • 0006611890 scopus 로고
    • Transmembrane signal transduction in bacterial chemotaxis involves ligand-dependent activation of phosphate group transfer
    • Borkovich, K. A., N. Kaplan, J. F. Hess, and M. I. Simon. 1989. Transmembrane signal transduction in bacterial chemotaxis involves ligand-dependent activation of phosphate group transfer. Proc. Natl. Acad. Sci. USA 86:1208-1212.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 1208-1212
    • Borkovich, K.A.1    Kaplan, N.2    Hess, J.F.3    Simon, M.I.4
  • 5
    • 0037151097 scopus 로고    scopus 로고
    • CheW binding interactions with CheA and Tar: Importance for chemotaxis signaling in Escherichia coli
    • Boukhvalova, M., F. W. Dahlquist, and R. C. Stewart. 2002. CheW binding interactions with CheA and Tar: importance for chemotaxis signaling in Escherichia coli. J. Biol. Chem. 277:22251-22259.
    • (2002) J. Biol. Chem. , vol.277 , pp. 22251-22259
    • Boukhvalova, M.1    Dahlquist, F.W.2    Stewart, R.C.3
  • 6
    • 0037189482 scopus 로고    scopus 로고
    • CheA kinase and chemoreceptor interaction surfaces on CheW
    • Boukhvalova, M., R. VanBruggen, and R. C. Stewart. 2002. CheA kinase and chemoreceptor interaction surfaces on CheW. J. Biol. Chem. 277:23596-23603.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23596-23603
    • Boukhvalova, M.1    VanBruggen, R.2    Stewart, R.C.3
  • 7
    • 0037155843 scopus 로고    scopus 로고
    • Molecular information processing: Lessons from bacterial chemotaxis
    • Bourret, R. B., and A. M. Stock. 2002. Molecular information processing: lessons from bacterial chemotaxis. J. Biol. Chem. 277:9625-9628.
    • (2002) J. Biol. Chem. , vol.277 , pp. 9625-9628
    • Bourret, R.B.1    Stock, A.M.2
  • 8
    • 0034460297 scopus 로고    scopus 로고
    • How signals are heard during bacterial chemotaxis: Protein-protein interactions in sensory signal propagation
    • Bren, A., and M. Eisenbach. 2000. How signals are heard during bacterial chemotaxis: protein-protein interactions in sensory signal propagation. J. Bacteriol. 182:6865-6873.
    • (2000) J. Bacteriol. , vol.182 , pp. 6865-6873
    • Bren, A.1    Eisenbach, M.2
  • 9
    • 0033106244 scopus 로고    scopus 로고
    • Evaluation and improvement of multiple sequence methods for protein secondary structure prediction
    • Cuff, J. A., and G. J. Barton. 1999. Evaluation and improvement of multiple sequence methods for protein secondary structure prediction. Proteins 34: 508-519.
    • (1999) Proteins , vol.34 , pp. 508-519
    • Cuff, J.A.1    Barton, G.J.2
  • 10
    • 0000228203 scopus 로고
    • A model of evolutionary change in proteins
    • M. O. Dayhoff, (ed.). National Biomedical Research Foundation, Washington, D.C.
    • Dayhoff, M. O., R. Schwartz, and B. C. Orcutt. 1978. A model of evolutionary change in proteins, p. 345-352. In M. O. Dayhoff, (ed.), Atlas of protein sequences and structures, vol. 5, Suppl. 3. National Biomedical Research Foundation, Washington, D.C.
    • (1978) Atlas of Protein Sequences and Structures , vol.5 , Issue.SUPPL. 3 , pp. 345-352
    • Dayhoff, M.O.1    Schwartz, R.2    Orcutt, B.C.3
  • 11
    • 0031455398 scopus 로고    scopus 로고
    • The two-component signaling pathway of bacterial chemotaxis: A molecular view of signal transduction by receptors, kinases, and adaptation enzymes
    • Falke, J. J., R. B. Bass, S. L. Butler, S. A. Chervitz, and M. A. Danielson. 1997. The two-component signaling pathway of bacterial chemotaxis: a molecular view of signal transduction by receptors, kinases, and adaptation enzymes. Annu. Rev. Cell Dev. Biol. 13:457-512.
    • (1997) Annu. Rev. Cell Dev. Biol. , vol.13 , pp. 457-512
    • Falke, J.J.1    Bass, R.B.2    Butler, S.L.3    Chervitz, S.A.4    Danielson, M.A.5
  • 13
    • 0026808410 scopus 로고
    • Assembly of an MCP receptor, CheW and kinase CheA complex in the bacterial chemotaxis signal transduction pathway
    • Gegner, J. A., D. R. Graham, A. F. Roth, and F. W. Dahlquist. 1992. Assembly of an MCP receptor, CheW and kinase CheA complex in the bacterial chemotaxis signal transduction pathway. Cell 70:975-982.
    • (1992) Cell , vol.70 , pp. 975-982
    • Gegner, J.A.1    Graham, D.R.2    Roth, A.F.3    Dahlquist, F.W.4
  • 16
    • 0037133375 scopus 로고    scopus 로고
    • A major chemotaxis gene cluster in Azospirillum brasilense and relationships between chemotaxis operons in α-proteobacteria
    • Hauwaerts, D., G. Alexandre, S. K. Das, J. Vanderleyden, and I. B. Zhulin. 2002. A major chemotaxis gene cluster in Azospirillum brasilense and relationships between chemotaxis operons in α-proteobacteria. FEMS Microbiol. Lett. 208:61-67.
    • (2002) FEMS Microbiol. Lett. , vol.208 , pp. 61-67
    • Hauwaerts, D.1    Alexandre, G.2    Das, S.K.3    Vanderleyden, J.4    Zhulin, I.B.5
  • 17
    • 0026458378 scopus 로고
    • Amino acid substitution matrices from protein blocks
    • Henikoff, S., and J. G. Henikoff. 1992. Amino acid substitution matrices from protein blocks. Proc. Natl. Acad. Sci. USA 89:10915-10919.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10915-10919
    • Henikoff, S.1    Henikoff, J.G.2
  • 18
    • 0024281410 scopus 로고
    • Phosphorylation of three proteins in the signaling pathway of bacterial chemotaxis
    • Hess, J. F., K. Oosawa, N. Kaplan, and M. I. Simon. 1988. Phosphorylation of three proteins in the signaling pathway of bacterial chemotaxis. Cell 53:79-87.
    • (1988) Cell , vol.53 , pp. 79-87
    • Hess, J.F.1    Oosawa, K.2    Kaplan, N.3    Simon, M.I.4
  • 20
    • 0030606898 scopus 로고    scopus 로고
    • Molecular evolution of the C-terminal cytoplasmic domain of a superfamily of bacterial receptors involved in taxis
    • Le Moual, H., and D. E. Koshland, Jr. 1996. Molecular evolution of the C-terminal cytoplasmic domain of a superfamily of bacterial receptors involved in taxis. J. Mol. Biol. 261:568-585.
    • (1996) J. Mol. Biol. , vol.261 , pp. 568-585
    • Le Moual, H.1    Koshland D.E., Jr.2
  • 21
    • 0024316868 scopus 로고
    • Role of CheW protein in coupling membrane receptors to the intracellular signaling system of bacterial chemotaxis
    • Liu, J., and J. S. Parkinson. 1989. Role of CheW protein in coupling membrane receptors to the intracellular signaling system of bacterial chemotaxis. Proc. Natl. Acad. Sci. USA 86:8703-8707.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8703-8707
    • Liu, J.1    Parkinson, J.S.2
  • 22
    • 0036134757 scopus 로고    scopus 로고
    • Heterotachy, an important process in protein evolution
    • Lopez, P., D. Casane, and H. Philippe. 2002. Heterotachy, an important process in protein evolution. Mol. Biol. Evol. 19:1-7.
    • (2002) Mol. Biol. Evol. , vol.19 , pp. 1-7
    • Lopez, P.1    Casane, D.2    Philippe, H.3
  • 23
    • 0033603635 scopus 로고    scopus 로고
    • Identification of the binding surfaces on CheY for two of its targets, the phosphatase CheZ and the flagellar switch protein FliM
    • McEvoy, M. M., A. Bren, M. Eisenbach, and F. W. Dahlquist. 1999. Identification of the binding surfaces on CheY for two of its targets, the phosphatase CheZ and the flagellar switch protein FliM. J. Mol. Biol. 289:1423-1433.
    • (1999) J. Mol. Biol. , vol.289 , pp. 1423-1433
    • McEvoy, M.M.1    Bren, A.2    Eisenbach, M.3    Dahlquist, F.W.4
  • 24
    • 0032560570 scopus 로고    scopus 로고
    • Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway
    • McEvoy, M. M., A. C. Hausrath, G. B. Randolph, S. J. Remington, and F. W. Dahlquist. 1998. Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway. Proc. Natl. Acad. Sci. USA 95:7333-7338.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7333-7338
    • McEvoy, M.M.1    Hausrath, A.C.2    Randolph, G.B.3    Remington, S.J.4    Dahlquist, F.W.5
  • 25
    • 0345062357 scopus 로고    scopus 로고
    • Universally conserved positions in protein folds: Reading evolutionary signals about stability, folding kinetics and function
    • Mirny, L. A., and E. I. Shakhnovich. 1999. Universally conserved positions in protein folds: reading evolutionary signals about stability, folding kinetics and function. J. Mol. Biol. 291:177-196.
    • (1999) J. Mol. Biol. , vol.291 , pp. 177-196
    • Mirny, L.A.1    Shakhnovich, E.I.2
  • 27
    • 0018189924 scopus 로고
    • Complementation analysis and deletion mapping of Escherichia coli mutants defective in chemotaxis
    • Parkinson, J. S. 1978. Complementation analysis and deletion mapping of Escherichia coli mutants defective in chemotaxis. J. Bacteriol. 135:45-53.
    • (1978) J. Bacteriol. , vol.135 , pp. 45-53
    • Parkinson, J.S.1
  • 28
    • 0035399936 scopus 로고    scopus 로고
    • On the conservation of protein sequences in evolution
    • Philippe, H., and P. Lopez. 2001. On the conservation of protein sequences in evolution. Trends Biochem. Sci. 26:414-416.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 414-416
    • Philippe, H.1    Lopez, P.2
  • 29
    • 0029889988 scopus 로고    scopus 로고
    • PHD: Predicting one-dimensional protein structure by profile-based neural networks
    • Rost, B. 1996. PHD: predicting one-dimensional protein structure by profile-based neural networks. Methods Enzymol. 266:525-539.
    • (1996) Methods Enzymol. , vol.266 , pp. 525-539
    • Rost, B.1
  • 31
    • 0024420315 scopus 로고
    • Role of the CheW protein in bacterial chemotaxis: Overexpression is equivalent to absence
    • Sanders, D. A., B. Mendez, and D. E. Koshland, Jr. 1989. Role of the CheW protein in bacterial chemotaxis: overexpression is equivalent to absence. J. Bacteriol. 171:6271-6278.
    • (1989) J. Bacteriol. , vol.171 , pp. 6271-6278
    • Sanders, D.A.1    Mendez, B.2    Koshland D.E., Jr.3
  • 32
    • 0036196317 scopus 로고    scopus 로고
    • Sensory transduction to the flagellar motor of Sinorhizobium meliloti
    • Scharf, B., and R. Schmitt. 2002. Sensory transduction to the flagellar motor of Sinorhizobium meliloti. J. Mol. Microbiol. Biotechnol. 4:183-186.
    • (2002) J. Mol. Microbiol. Biotechnol. , vol.4 , pp. 183-186
    • Scharf, B.1    Schmitt, R.2
  • 33
    • 0033977153 scopus 로고    scopus 로고
    • Identification of a fourth cheY gene in Rhodobacter sphaeroides and interspecies interaction within the bacterial signal transduction pathway
    • Shah, D. S. H., S. L. Porter, D. C. Harris, G. H. Wadhams, P. A. Hamblin, and J. P. Armitage. 2000. Identification of a fourth cheY gene in Rhodobacter sphaeroides and interspecies interaction within the bacterial signal transduction pathway. Mol. Microbiol. 35:101-112.
    • (2000) Mol. Microbiol. , vol.35 , pp. 101-112
    • Shah, D.S.H.1    Porter, S.L.2    Harris, D.C.3    Wadhams, G.H.4    Hamblin, P.A.5    Armitage, J.P.6
  • 34
    • 14444278048 scopus 로고    scopus 로고
    • Flagellar motor-switch binding face of CheY and the biochemical basis of suppression by CheY mutants that compensate for motor-switch defects in Escherichia coli
    • Shulda, D., X. Y. Zhu, and P. Matsumura. 1998. Flagellar motor-switch binding face of CheY and the biochemical basis of suppression by CheY mutants that compensate for motor-switch defects in Escherichia coli. J. Biol. Chem. 273:23993-23999.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23993-23999
    • Shulda, D.1    Zhu, X.Y.2    Matsumura, P.3
  • 35
    • 0035947730 scopus 로고    scopus 로고
    • Alteration of a nonconserved active site residue in the chemotaxis response regulator CheY affects phosphorylation and interaction with CheZ
    • Silversmith, R. E., J. G. Smith, G. P. Guanga, J. T. Les, and R. B. Bourret. 2001. Alteration of a nonconserved active site residue in the chemotaxis response regulator CheY affects phosphorylation and interaction with CheZ. J. Biol. Chem. 276:18478-18484.
    • (2001) J. Biol. Chem. , vol.276 , pp. 18478-18484
    • Silversmith, R.E.1    Smith, J.G.2    Guanga, G.P.3    Les, J.T.4    Bourret, R.B.5
  • 36
    • 0037022603 scopus 로고    scopus 로고
    • Inference of functional regions in proteins by quantification of evolutionary constraints
    • Simon, A. L., E. A. Stone, and A. Sidow, 2002. Inference of functional regions in proteins by quantification of evolutionary constraints. Proc. Natl. Acad. Sci. USA 99:2912-2917.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 2912-2917
    • Simon, A.L.1    Stone, E.A.2    Sidow, A.3
  • 37
    • 0033792542 scopus 로고    scopus 로고
    • Rapid phosphotransfer to CheY from a CheA protein lacking the CheY-binding domain
    • Stewart, R. C., K. Jahreis, and J. S. Parkinson. 2000. Rapid phosphotransfer to CheY from a CheA protein lacking the CheY-binding domain. Biochemistry 39:13157-13165.
    • (2000) Biochemistry , vol.39 , pp. 13157-13165
    • Stewart, R.C.1    Jahreis, K.2    Parkinson, J.S.3
  • 38
    • 0032964297 scopus 로고    scopus 로고
    • BLAST 2 sequences, a new tool for comparing protein and nucleotide sequences
    • Tatusova, T. A., and T. L. Madden. 1999. BLAST 2 sequences, a new tool for comparing protein and nucleotide sequences. FEMS Microbiol. Lett. 174: 247-250.
    • (1999) FEMS Microbiol. Lett. , vol.174 , pp. 247-250
    • Tatusova, T.A.1    Madden, T.L.2
  • 39
    • 0036306115 scopus 로고    scopus 로고
    • Why are proteins so robust to site mutations?
    • Taverna, D. M., and R. A. Goldstein. 2002. Why are proteins so robust to site mutations? J. Mol. Biol. 315:479-484.
    • (2002) J. Mol. Biol. , vol.315 , pp. 479-484
    • Taverna, D.M.1    Goldstein, R.A.2
  • 40
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X Windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J. D., T. J. Gibson, F. Plewniak, F. Jeanmougin, and D. G. Higgins. 1997. The CLUSTAL_X Windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25:4876-4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 41
    • 0025741662 scopus 로고
    • Crystal structure of Escherichia coli CheY refined at 1.7-Å resolution
    • Volz, K., and P. Matsumura. 1991. Crystal structure of Escherichia coli CheY refined at 1.7-Å resolution. J. Biol. Chem. 266:15511-15519.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15511-15519
    • Volz, K.1    Matsumura, P.2
  • 42
    • 0031975752 scopus 로고    scopus 로고
    • Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY
    • Welch, M., N. Chinardet, L. Mourey, C. Birck, and J.-P. Samama. 1998. Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY. Nat. Struct. Biol. 5:25-29.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 25-29
    • Welch, M.1    Chinardet, N.2    Mourey, L.3    Birck, C.4    Samama, J.-P.5
  • 43
    • 0027517812 scopus 로고
    • Phosphorylation-dependent binding of a signal molecule to the flagellar switch of bacteria
    • Welch, M., K. Oosawa, S. Aizawa, and M. Eisenbach. 1993. Phosphorylation-dependent binding of a signal molecule to the flagellar switch of bacteria. Proc. Natl. Acad. Sci. USA 90:8787-8791.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8787-8791
    • Welch, M.1    Oosawa, K.2    Aizawa, S.3    Eisenbach, M.4
  • 44
    • 0007809063 scopus 로고
    • Migration of bacteria in semisolid agar
    • Wolfe, A. J., and H. C, Berg. 1989. Migration of bacteria in semisolid agar. Proc. Natl. Acad. Sci. USA 86:6973-6977.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 6973-6977
    • Wolfe, A.J.1    Berg, H.C.2
  • 45
    • 0036312369 scopus 로고    scopus 로고
    • Structure and catalytic mechanism of the E. coli chemotaxis phosphatase CheZ
    • Zhao, R., E. J. Collins, R. B. Bourret, and R. E. Silversmith. 2002. Structure and catalytic mechanism of the E. coli chemotaxis phosphatase CheZ. Nat. Struct. Biol. 9:570-575.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 570-575
    • Zhao, R.1    Collins, E.J.2    Bourret, R.B.3    Silversmith, R.E.4
  • 46
    • 0034964703 scopus 로고    scopus 로고
    • Thc superfamily of chemotaxis transducers: From physiology to genomics and back
    • Zhulin, I. B. 2001. Thc superfamily of chemotaxis transducers: from physiology to genomics and back. Adv. Microb. Physiol. 45:157-198.
    • (2001) Adv. Microb. Physiol. , vol.45 , pp. 157-198
    • Zhulin, I.B.1


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