Literature DB >> 10066483

Signal transduction in bacteria: molecular mechanisms of stimulus-response coupling.

P N Goudreau1, A M Stock.   

Abstract

In bacteria, adaptive responses to changing environmental conditions are mediated by signal transduction systems that involve modular protein domains. Despite great diversity in the integration of domains into different systems, studies of individual components have revealed molecular strategies that are widely applicable. Studies of receptors have advanced our understanding of how information is transmitted across membranes, the determination of three-dimensional structures of domains of histidine protein kinase domains and response regulator proteins has begun to reveal the molecular basis of signaling via two-component phosphoryltransfer pathways, and the description of 'eukaryotic-like' protein domains involved in bacterial signaling has emphasized the universality of intracellular signaling mechanisms.

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Year:  1998        PMID: 10066483     DOI: 10.1016/s1369-5274(98)80006-4

Source DB:  PubMed          Journal:  Curr Opin Microbiol        ISSN: 1369-5274            Impact factor:   7.934


  15 in total

1.  Clustering of the chemoreceptor complex in Escherichia coli is independent of the methyltransferase CheR and the methylesterase CheB.

Authors:  S R Lybarger; J R Maddock
Journal:  J Bacteriol       Date:  1999-09       Impact factor: 3.490

2.  Chemistry and biology.

Authors:  G A Petsko
Journal:  Proc Natl Acad Sci U S A       Date:  2000-01-18       Impact factor: 11.205

Review 3.  PAS domains: internal sensors of oxygen, redox potential, and light.

Authors:  B L Taylor; I B Zhulin
Journal:  Microbiol Mol Biol Rev       Date:  1999-06       Impact factor: 11.056

4.  High genetic variability of the agr locus in Staphylococcus species.

Authors:  Philippe Dufour; Sophie Jarraud; Francois Vandenesch; Timothy Greenland; Richard P Novick; Michele Bes; Jerome Etienne; Gerard Lina
Journal:  J Bacteriol       Date:  2002-02       Impact factor: 3.490

5.  Structural insight into the low affinity between Thermotoga maritima CheA and CheB compared to their Escherichia coli/Salmonella typhimurium counterparts.

Authors:  Sangyoun Park; Brian R Crane
Journal:  Int J Biol Macromol       Date:  2011-07-23       Impact factor: 6.953

6.  Structure of the ternary complex formed by a chemotaxis receptor signaling domain, the CheA histidine kinase, and the coupling protein CheW as determined by pulsed dipolar ESR spectroscopy.

Authors:  Jaya Bhatnagar; Peter P Borbat; Abiola M Pollard; Alexandrine M Bilwes; Jack H Freed; Brian R Crane
Journal:  Biochemistry       Date:  2010-05-11       Impact factor: 3.162

7.  An insight into the interaction mode between CheB and chemoreceptor from two crystal structures of CheB methylesterase catalytic domain.

Authors:  Kwang-Hwi Cho; Brian R Crane; Sangyoun Park
Journal:  Biochem Biophys Res Commun       Date:  2011-06-21       Impact factor: 3.575

8.  The TorR high-affinity binding site plays a key role in both torR autoregulation and torCAD operon expression in Escherichia coli.

Authors:  M Ansaldi; G Simon; M Lepelletier; V Méjean
Journal:  J Bacteriol       Date:  2000-02       Impact factor: 3.490

9.  Characterization of the vanD glycopeptide resistance gene cluster from Enterococcus faecium BM4339.

Authors:  B Casadewall; P Courvalin
Journal:  J Bacteriol       Date:  1999-06       Impact factor: 3.490

10.  In different organisms, the mode of interaction between two signaling proteins is not necessarily conserved.

Authors:  Sang-Youn Park; Bryan D Beel; Melvin I Simon; Alexandrine M Bilwes; Brian R Crane
Journal:  Proc Natl Acad Sci U S A       Date:  2004-08-02       Impact factor: 11.205

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