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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Gene Review

ECs0449  -  transcriptional regulator PhoB

Escherichia coli O157:H7 str. Sakai

 
 
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Disease relevance of ECs0449

 

High impact information on ECs0449

  • Phosphorylated PhoB, which binds to the pho promoters with high affinity, mediated the specific binding of the wild-type holoenzyme to the pstS promoter, but it did not mediate the binding of the mutant holoenzymes [1].
  • These results suggest that PhoB promotes specific interaction between RNA polymerase and the pho promoters for transcriptional activation, and the first helix of the putative HTH motif plays an essential role in the interaction, probably by making direct contact with PhoB [1].
  • A common switch in activation of the response regulators NtrC and PhoB: phosphorylation induces dimerization of the receiver modules [6].
  • Analysis of these hybrid proteins shows that the receiver modules of NtrC and PhoB are potential dimerization domains [6].
  • Conditionally replicative oriRR6K gamma attP "genome targeting" suicide plasmids carrying mutagenized phoB coding regions were integrated into the chromosome of a reporter strain to create mutant libraries; plasmids encoding mutant PhoB proteins were subsequently retrieved by P1-Int-Xis cloning [7].
 

Chemical compound and disease context of ECs0449

  • Transcription of the genes belonging to the phosphate (pho) regulon in Escherichia coli, which are induced by phosphate starvation, requires the specific activator protein PhoB in addition to the RNA polymerase holoenzyme containing the major sigma-factor sigma 70 [1].
  • In this report, we demonstrate that the cytoplasmic domain of VanS (including residues Met95 to Ser384) is capable of high level activation (> 500 fold) of the Escherichia coli response regulator PhoB in vivo in the absence of its signaling kinases PhoR, CreC (PhoM), or acetyl phosphate synthesis [8].
  • Cross talk to the phosphate regulon of Escherichia coli by PhoM protein: PhoM is a histidine protein kinase and catalyzes phosphorylation of PhoB and PhoM-open reading frame 2 [9].
  • Dual transcriptional regulation of the Escherichia coli phosphate-starvation-inducible psiE gene of the phosphate regulon by PhoB and the cyclic AMP (cAMP)-cAMP receptor protein complex [10].
 

Biological context of ECs0449

  • We present here the DNA sequence of the phoP gene and show that the deduced amino acid sequence of phoP has extensive homology with the Escherichia coli transcriptional regulators PhoB and OmpR, which control the expression of loci in response to different environmental stimuli [11].
  • The two-component regulatory pair PhoR/PhoB is responsible for upregulation of Pho regulon expression in response to P(i)-limiting environments [12].
  • PhoB is the response regulator of the two-component signal transduction system activated under phosphate starvation conditions [13].
  • Mutagenesis studies performed on several members of this family, OmpR, PhoB, ToxR and VirG, can now be interpreted with respect to the structure [14].
  • The binding site of PhoB is a TGTCA sequence and the phospahte box contains the two binding sites [15].
 

Associations of ECs0449 with chemical compounds

  • Activities of the pho promoters in vivo were severely reduced in these mutants, whereas those of the PhoB-independent promoters were affected only marginally at most [1].
  • Using a reporter strain synthesizing the nonpartner kinase VanS under tight arabinose control and carrying a promoter-lacZ fusion activated by phospho-PhoB, we isolated altered recognition (AR) mutants of PhoB showing enhanced activation (phosphorylation) by VanS as arabinose-dependent Lac+ mutants [7].
  • Several bacterial response regulator proteins (CheY, NRI, PhoB, and OmpR) become phosphorylated in vitro when incubated with acetyl phosphate [16].
  • Cross-talk between the histidine protein kinase VanS and the response regulator PhoB. Characterization and identification of a VanS domain that inhibits activation of PhoB [8].
  • The activation of PhoB by acetylphosphate [17].
 

Analytical, diagnostic and therapeutic context of ECs0449

  • In addition, when PhoB was phosphorylated by acetylphosphate it eluted from a high-performance liquid chromatography (HPLC) size-exclusion column in two peaks [17].
  • Site-directed mutagenesis revealed that one of these deviations, i.e. Leu-172, which is Arg in E. coli PhoB, is responsible for the lack of expression of the PhoE protein in S. flexneri [18].
  • Overexpression, purification, crystallization and preliminary X-ray diffraction analysis of the receiver domain of PhoB [19].
  • Among the 18 new putative genes that were found to be under the control of the PhoB transcriptional regulator, five genes that contain the consensus Pho box were identified by sequence analysis [20].
  • We present crystallography and solution NMR data for the receiver domain of Escherichia coli PhoB which show distinct 2-fold symmetric dimers in the inactive and active states [21].

References

  1. Role of the sigma 70 subunit of RNA polymerase in transcriptional activation by activator protein PhoB in Escherichia coli. Makino, K., Amemura, M., Kim, S.K., Nakata, A., Shinagawa, H. Genes Dev. (1993) [Pubmed]
  2. Crystal structure of the response regulator 02 receiver domain, the essential YycF two-component system of Streptococcus pneumoniae in both complexed and native states. Bent, C.J., Isaacs, N.W., Mitchell, T.J., Riboldi-Tunnicliffe, A. J. Bacteriol. (2004) [Pubmed]
  3. The crystal structure of the phosphorylation domain in PhoP reveals a functional tandem association mediated by an asymmetric interface. Birck, C., Chen, Y., Hulett, F.M., Samama, J.P. J. Bacteriol. (2003) [Pubmed]
  4. Inorganic polyphosphate in Escherichia coli: the phosphate regulon and the stringent response. Rao, N.N., Liu, S., Kornberg, A. J. Bacteriol. (1998) [Pubmed]
  5. Characterization of a two-component signal transduction system involved in the induction of alkaline phosphatase under phosphate-limiting conditions in Synechocystis sp. PCC 6803. Hirani, T.A., Suzuki, I., Murata, N., Hayashi, H., Eaton-Rye, J.J. Plant Mol. Biol. (2001) [Pubmed]
  6. A common switch in activation of the response regulators NtrC and PhoB: phosphorylation induces dimerization of the receiver modules. Fiedler, U., Weiss, V. EMBO J. (1995) [Pubmed]
  7. Altered recognition mutants of the response regulator PhoB: a new genetic strategy for studying protein-protein interactions. Haldimann, A., Prahalad, M.K., Fisher, S.L., Kim, S.K., Walsh, C.T., Wanner, B.L. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  8. Cross-talk between the histidine protein kinase VanS and the response regulator PhoB. Characterization and identification of a VanS domain that inhibits activation of PhoB. Fisher, S.L., Jiang, W., Wanner, B.L., Walsh, C.T. J. Biol. Chem. (1995) [Pubmed]
  9. Cross talk to the phosphate regulon of Escherichia coli by PhoM protein: PhoM is a histidine protein kinase and catalyzes phosphorylation of PhoB and PhoM-open reading frame 2. Amemura, M., Makino, K., Shinagawa, H., Nakata, A. J. Bacteriol. (1990) [Pubmed]
  10. Dual transcriptional regulation of the Escherichia coli phosphate-starvation-inducible psiE gene of the phosphate regulon by PhoB and the cyclic AMP (cAMP)-cAMP receptor protein complex. Kim, S.K., Kimura, S., Shinagawa, H., Nakata, A., Lee, K.S., Wanner, B.L., Makino, K. J. Bacteriol. (2000) [Pubmed]
  11. Salmonella typhimurium phoP virulence gene is a transcriptional regulator. Groisman, E.A., Chiao, E., Lipps, C.J., Heffron, F. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  12. Expression of the Pho regulon negatively regulates biofilm formation by Pseudomonas aureofaciens PA147-2. Monds, R.D., Silby, M.W., Mahanty, H.K. Mol. Microbiol. (2001) [Pubmed]
  13. Three-dimensional crystal structure of the transcription factor PhoB receiver domain. Solá, M., Gomis-Rüth, F.X., Serrano, L., González, A., Coll, M. J. Mol. Biol. (1999) [Pubmed]
  14. Structural relationships in the OmpR family of winged-helix transcription factors. Martínez-Hackert, E., Stock, A.M. J. Mol. Biol. (1997) [Pubmed]
  15. Structural comparison of the PhoB and OmpR DNA-binding/transactivation domains and the arrangement of PhoB molecules on the phosphate box. Okamura, H., Hanaoka, S., Nagadoi, A., Makino, K., Nishimura, Y. J. Mol. Biol. (2000) [Pubmed]
  16. Acetyl phosphate and the activation of two-component response regulators. McCleary, W.R., Stock, J.B. J. Biol. Chem. (1994) [Pubmed]
  17. The activation of PhoB by acetylphosphate. McCleary, W.R. Mol. Microbiol. (1996) [Pubmed]
  18. The pho regulon of Shigella flexneri. Scholten, M., Janssen, R., Bogaarts, C., van Strien, J., Tommassen, J. Mol. Microbiol. (1995) [Pubmed]
  19. Overexpression, purification, crystallization and preliminary X-ray diffraction analysis of the receiver domain of PhoB. Sol, M., Gomis-Rüth, F., Guasch, A., Serrano, L., Coll, M. Acta Crystallogr. D Biol. Crystallogr. (1998) [Pubmed]
  20. Novel gene members in the Pho regulon of Escherichia coli. Baek, J.H., Lee, S.Y. FEMS Microbiol. Lett. (2006) [Pubmed]
  21. Mechanism of activation for transcription factor PhoB suggested by different modes of dimerization in the inactive and active states. Bachhawat, P., Swapna, G.V., Montelione, G.T., Stock, A.M. Structure (Camb.) (2005) [Pubmed]
 
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