Literature DB >> 12015152

Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator.

Alexandre G Blanco1, Maria Sola, F Xavier Gomis-Rüth, Miquel Coll.   

Abstract

PhoB is a signal transduction response regulator that activates nearly 40 genes in phosphate depletion conditions in E. coli and closely related bacteria. The structure of the PhoB effector domain in complex with its target DNA sequence, or pho box, reveals a novel tandem arrangement in which several monomers bind head to tail to successive 11-base pair direct-repeat sequences, coating one face of a smoothly bent double helix. The protein has a winged helix fold in which the DNA recognition elements comprise helix alpha 3, penetrating the major groove, and a beta hairpin wing interacting with a compressed minor groove via Arg219, tightly sandwiched between the DNA sugar backbones. The transactivation loops protrude laterally in an appropriate orientation to interact with the RNA polymerase sigma(70) subunit, which triggers transcription initiation.

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Year:  2002        PMID: 12015152     DOI: 10.1016/s0969-2126(02)00761-x

Source DB:  PubMed          Journal:  Structure        ISSN: 0969-2126            Impact factor:   5.006


  140 in total

1.  Residue R113 is essential for PhoP dimerization and function: a residue buried in the asymmetric PhoP dimer interface determined in the PhoPN three-dimensional crystal structure.

Authors:  Yinghua Chen; Catherine Birck; Jean-Pierre Samama; F Marion Hulett
Journal:  J Bacteriol       Date:  2003-01       Impact factor: 3.490

2.  The crystal structure of the phosphorylation domain in PhoP reveals a functional tandem association mediated by an asymmetric interface.

Authors:  Catherine Birck; Yinghua Chen; F Marion Hulett; Jean-Pierre Samama
Journal:  J Bacteriol       Date:  2003-01       Impact factor: 3.490

3.  Increased Pho regulon activation correlates with decreased virulence of an avian pathogenic Escherichia coli O78 strain.

Authors:  Nicolas Bertrand; Sébastien Houle; Guillaume LeBihan; Édith Poirier; Charles M Dozois; Josée Harel
Journal:  Infect Immun       Date:  2010-10-04       Impact factor: 3.441

4.  Structure of the response regulator PhoP from Mycobacterium tuberculosis reveals a dimer through the receiver domain.

Authors:  Smita Menon; Shuishu Wang
Journal:  Biochemistry       Date:  2011-06-13       Impact factor: 3.162

5.  Phosphorylation of PhoP protein plays direct regulatory role in lipid biosynthesis of Mycobacterium tuberculosis.

Authors:  Rajni Goyal; Arijit Kumar Das; Ranjeet Singh; Pradip K Singh; Suresh Korpole; Dibyendu Sarkar
Journal:  J Biol Chem       Date:  2011-11-09       Impact factor: 5.157

6.  Solution structure and DNA binding of the effector domain from the global regulator PrrA (RegA) from Rhodobacter sphaeroides: insights into DNA binding specificity.

Authors:  Cédric Laguri; Mary K Phillips-Jones; Michael P Williamson
Journal:  Nucleic Acids Res       Date:  2003-12-01       Impact factor: 16.971

7.  Regulation of sialic acid catabolism by the DNA binding protein NanR in Escherichia coli.

Authors:  Kathryn A Kalivoda; Susan M Steenbergen; Eric R Vimr; Jacqueline Plumbridge
Journal:  J Bacteriol       Date:  2003-08       Impact factor: 3.490

8.  Experimental maps of DNA structure at nucleotide resolution distinguish intrinsic from protein-induced DNA deformations.

Authors:  Robert N Azad; Dana Zafiropoulos; Douglas Ober; Yining Jiang; Tsu-Pei Chiu; Jared M Sagendorf; Remo Rohs; Thomas D Tullius
Journal:  Nucleic Acids Res       Date:  2018-03-16       Impact factor: 16.971

9.  An Iterative, Synthetic Approach To Engineer a High-Performance PhoB-Specific Reporter.

Authors:  Julie L Stoudenmire; Tara Essock-Burns; Erena N Weathers; Sina Solaimanpour; Jan Mrázek; Eric V Stabb
Journal:  Appl Environ Microbiol       Date:  2018-07-02       Impact factor: 4.792

10.  Phosphorylation-dependent derepression by the response regulator HnoC in the Shewanella oneidensis nitric oxide signaling network.

Authors:  Lars Plate; Michael A Marletta
Journal:  Proc Natl Acad Sci U S A       Date:  2013-11-11       Impact factor: 11.205

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