Two-Component Signaling Systems

Part of the Biological and Medical Physics, Biomedical Engineering book series (BIOMEDICAL)


Response Regulator Histidine Kinase Phosphoryl Group Bacterial Chemotaxis Conserve Histidine Residue 
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References and Further Reading

Histidine Kinases

  1. Bilwes AM, et al. [1999]. Structure of CheA, a signal-transducing histidine kinase. Cell, 96: 131–141.CrossRefGoogle Scholar
  2. Mourey L, et al. [2001]. Crystal structure of the CheA histidine phosphotransfer domain that mediates response regulator phosphorylation in bacterial chemotaxis. J. Biol. Chem., 276: 31074–31082.CrossRefGoogle Scholar

Response Regulators

  1. Baikalov I, et al. [1996]. Structure of the Escherichia coli response regulator NarL. Biochem., 35: 11053–11061.CrossRefGoogle Scholar
  2. Birch C, et al. [1999]. Conformational changes induced by phosphorylation of the FixJ receiver domain. Structure, 7: 1505–1515.CrossRefGoogle Scholar
  3. Feher VA, and Cavanagh J [1999]. Millisecond-timescale motions contribute to the function of the bacterial response regulator protein Spo0F. Nature, 400: 289–293.CrossRefADSGoogle Scholar
  4. Kern D, et al. [1999]. Structure of a transiently phosphorylated switch in bacterial signal transduction. Nature, 402: 894–898.CrossRefADSGoogle Scholar
  5. Lewis RJ, et al. [1999]. Phosphorylated aspartate in the structure of a response regulator protein. J. Mol. Biol., 294: 9–15.CrossRefGoogle Scholar
  6. Stock J, and Da Re S [2000]. Signal transduction: Response regulators on and off. Curr. Biol., 10: R420–R424.CrossRefGoogle Scholar
  7. Volkman BF, et al. [2001]. Two-state allosteric behavior in a single-domain signaling protein. Science, 291: 2429–2433.CrossRefADSGoogle Scholar

Chemotaxis Receptors

  1. Falke JJ, and Hazelbauer GL [2001]. Transmembrane signaling in bacterial chemoreceptors. Trends Biochem. Sci., 26: 257–265.CrossRefGoogle Scholar
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  3. Ottemann KM, et al. [1999]. A piston model for transmembrane signaling of the aspartate receptor. Science, 285: 1751–1754.CrossRefGoogle Scholar
  4. West AH, and Stock AM [2001]. Histidine kinases and response regulator proteins in two-component signaling systems. Trends Biochem. Sci., 26: 369–376.CrossRefGoogle Scholar
  5. Volz K [1993]. Structural conservation in the CheY superfamily. Biochem., 32: 11741–11753.CrossRefGoogle Scholar

Feedback, Methylation, and Robust Behavior

  1. Barkai N, and Leibler S [1997]. Robustness in simple chemical networks. Nature, 387: 913–917.CrossRefADSGoogle Scholar
  2. Djordjevic S, et al. [1998]. Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain. Proc. Natl. Acad. Sci. USA, 95: 1381–1386.CrossRefADSGoogle Scholar
  3. Djordjevic S, and Stock AM [1997]. Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding Sadenosylmethionine. Structure, 5: 545–558.CrossRefGoogle Scholar
  4. Yi TM, Huang Y, Simon MI, and Doyle J [2000]. Robust perfect adaptation in bacterial chemotaxis through integral feedback control. Proc. Natl. Acad. Sci. USA, 97: 4649–4653.CrossRefADSGoogle Scholar

Receptor Clusters and Formation of a Primitive Nose

  1. Liu Y, et al. [1997]. Receptor-mediated protein kinase activation and mechanism of transmembrane signaling in bacterial chemotaxis. EMBO J., 16: 7231–7240.CrossRefGoogle Scholar
  2. Levit MN, Liu Y, and Stock JB [1998]. Stimulus response coupling in bacterial chemotaxis: Receptor dimers in signaling arrays. Mol. Microbiol., 30: 459–466.CrossRefGoogle Scholar
  3. Duke TAJ, and Bray D [1999]. Heightened sensitivity of a lattice of membrane receptors. Proc. Natl. Acad. Sci. USA, 96: 10104–10108.CrossRefADSGoogle Scholar
  4. Shimizu TS, et al. [2000]. Molecular model of a lattice of signaling proteins involved in bacterial chemotaxis. Nature Cell Biol., 2: 792–796.CrossRefGoogle Scholar

Plant His-Asp Signaling

  1. Cashmore AR, et al. [1999]. Cryptochromes: Blue light receptors for plants and animals. Science, 284: 760–765.CrossRefADSGoogle Scholar
  2. Lohrmann J, and Harter K [2002]. Plant two-component signaling systems and the role of response regulators. Plant Physiol., 128: 363–369.CrossRefGoogle Scholar
  3. Neff MM, Fankhauser C, and Chory J [2000]. Light: An indicator of time and place. Genes Dev., 14: 257–271.Google Scholar
  4. Smith H [2000]. Phytochromes and light signal perception by plants-An emerging synthesis. Nature, 407: 585–591.CrossRefADSGoogle Scholar
  5. Young MW, and Kay SA [2001]. Time zones: A comparative genetics of circadian clocks. Nat. Rev. Genet., 2: 702–715.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, Inc. 2005

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