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Two-Component Signaling Systems

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

Keywords

Response Regulator Histidine Kinase Phosphoryl Group Bacterial Chemotaxis Conserve Histidine Residue 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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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
  2. Mowbray SL, and Sandgren MOJ [1998]. Chemotaxis receptors: A progress report on structure and function. J. Struct. Biol., 124: 257–275.CrossRefGoogle Scholar
  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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