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Gene Review

abrB  -  AbrB protein

Escherichia coli CFT073

 
 
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Disease relevance of abrB

 

High impact information on abrB

  • These findings reinforce the hypothesis that AbrB represses gene expression through its direct interaction with the transcription initiation regions of genes under its control [1].
  • AbrB protein was also observed to bind to the tycA gene within a region between the transcription start site and the tycA coding sequence as well as to a region containing the putative tycA promoter [1].
  • Spo0A binds to specific DNA sequences (0A boxes), and two such boxes are found downstream of the tandem promoters for the abrB gene [4].
  • The regulated expression of this operon by Spo0A-P is mediated indirectly through the transition state regulator AbrB and is manifest only during growth on solid medium [5].
  • In fact, purified AbrB protein bound to a portion of the dciA promoter region, protecting it against DNase I digestion [6].
 

Biological context of abrB

  • The abrupt reduction of abrB transcript level during the early period of the growth cycle is effected by the phosphorylated form of the response regulator Spo0p3and to a lesser extent by negative autoregulation [2].
  • The dependence on the spo0A gene product could be entirely bypassed by an abrB suppressor mutation, which caused tycA-lacZ to be transcribed constitutively at all stages of growth [7].
  • We hypothesize therefore that AbrB, like Fis, is a nucleoid binding protein [2].
  • The global regulators AbrB, Abh, and SpoVT are paralogous proteins showing their most extensive sequence homologies in the DNA-binding amino-terminal regions (about 50 residues) [8].
  • The Bacillus subtilis global transition-state regulator AbrB specifically recognizes over 60 different DNA regulatory regions of genes expressed during cellular response to suboptimal environments [9].
 

Associations of abrB with chemical compounds

  • Expression of dciA in growing cells was also repressed independently by glucose and by a mixture of amino acids; neither of these effects was mediated by AbrB [6].

References

  1. AbrB, a regulator of gene expression in Bacillus, interacts with the transcription initiation regions of a sporulation gene and an antibiotic biosynthesis gene. Robertson, J.B., Gocht, M., Marahiel, M.A., Zuber, P. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  2. Expression of AbrB, a transition state regulator from Bacillus subtilis, is growth phase dependent in a manner resembling that of Fis, the nucleoid binding protein from Escherichia coli. O'Reilly, M., Devine, K.M. J. Bacteriol. (1997) [Pubmed]
  3. Molecular characterization of the transition state regulator AbrB from Bacillus stearothermophilus. Klein, W., Winkelmann, D., Hahn, M., Weber, T., Marahiel, M.A. Biochim. Biophys. Acta (2000) [Pubmed]
  4. The Spo0A protein of Bacillus subtilis inhibits transcription of the abrB gene without preventing binding of the polymerase to the promoter. Greene, E.A., Spiegelman, G.B. J. Biol. Chem. (1996) [Pubmed]
  5. The citrulline biosynthetic operon, argC-F, and a ribose transport operon, rbs, from Bacillus subtilis are negatively regulated by Spo0A. O'Reilly, M., Woodson, K., Dowds, B.C., Devine, K.M. Mol. Microbiol. (1994) [Pubmed]
  6. Transcriptional regulation of a Bacillus subtilis dipeptide transport operon. Slack, F.J., Mueller, J.P., Strauch, M.A., Mathiopoulos, C., Sonenshein, A.L. Mol. Microbiol. (1991) [Pubmed]
  7. Identification of the promoter for a peptide antibiotic biosynthesis gene from Bacillus brevis and its regulation in Bacillus subtilis. Marahiel, M.A., Zuber, P., Czekay, G., Losick, R. J. Bacteriol. (1987) [Pubmed]
  8. Independent and interchangeable multimerization domains of the AbrB, Abh, and SpoVT global regulatory proteins. Yao, F., Strauch, M.A. J. Bacteriol. (2005) [Pubmed]
  9. Macromolecular assembly of the transition state regulator AbrB in its unbound and complexed states probed by microelectrospray ionization mass spectrometry. Benson, L.M., Vaughn, J.L., Strauch, M.A., Bobay, B.G., Thompson, R., Naylor, S., Cavanagh, J. Anal. Biochem. (2002) [Pubmed]
 
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