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Gene Review

blaR1  -  BlaR1

Staphylococcus aureus

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Disease relevance of blaR1

  • We report herein a kinetic and structural study, obtained by stopped-flow IR spectroscopy, of the activation of the BlaR1 receptor of the Staphylococcus aureus bacterium by beta-lactam antibiotics [1].

High impact information on blaR1

  • The cell-surface BlaR1 receptor alerts the bacterium to the presence of beta-lactam antibiotics, resulting in expression of the gene for a beta-lactamase enzyme [1].
  • The key chemical events in beta-lactam recognition are serine acylation and subsequent irreversible decarboxylation of the BlaR1 active site lysine carbamate [1].
  • Discrete steps in sensing of beta-lactam antibiotics by the BlaR1 protein of the methicillin-resistant Staphylococcus aureus bacterium [1].
  • Surprisingly, conformational changes upon penicillin binding were not observed in our structures, supporting the hypothesis that transduction of the antibiotic-binding signal into the cytosol is mediated by additional intramolecular interactions of the sensor domain with an adjacent extracellular loop in BlaR1 [2].
  • The beta-lactam sensor-transducer (BlaR), an integral membrane protein, binds beta-lactam antibiotics on the cell surface and transduces the information to the cytoplasm, where gene expression is derepressed for both beta-lactamase and penicillin-binding protein 2a [3].

Chemical compound and disease context of blaR1


Biological context of blaR1

  • As such, BlaR1 experience acylation by the antibiotic that it senses, an event that enjoys longevity for at least the duration of one bacterial generation [4].
  • The structure of the surface domain of the BlaR1 protein of Staphylococcus aureus, a beta-lactam antibiotic sensor/signal transducer, is essentially identical to that of the class D beta-lactamases, which are antibiotic resistance enzymes [4].
  • Two residues of the BlaR C-terminal domain, Thr452 and Thr542, modify the hydrophobic characteristic of the class D beta-lactamase active site [5].

Associations of blaR1 with chemical compounds

  • We report herein the production of S-(4-butanoate)-cysteine, as a surrogate of N-carboxylated lysine at position 392 of the BlaR1 protein [4].
  • Therefore we investigated the possibility that BlaR1 might be the main target for PDO action [6].
  • Our results demonstrate that BlaR1 could be an attractive new target for the development of new drugs to overcome methicillin resistance [6].


  1. Discrete steps in sensing of beta-lactam antibiotics by the BlaR1 protein of the methicillin-resistant Staphylococcus aureus bacterium. Thumanu, K., Cha, J., Fisher, J.F., Perrins, R., Mobashery, S., Wharton, C. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  2. Crystal structures of the Apo and penicillin-acylated forms of the BlaR1 beta-lactam sensor of Staphylococcus aureus. Wilke, M.S., Hills, T.L., Zhang, H.Z., Chambers, H.F., Strynadka, N.C. J. Biol. Chem. (2004) [Pubmed]
  3. Resistance to beta-lactam antibiotics and its mediation by the sensor domain of the transmembrane BlaR signaling pathway in Staphylococcus aureus. Golemi-Kotra, D., Cha, J.Y., Meroueh, S.O., Vakulenko, S.B., Mobashery, S. J. Biol. Chem. (2003) [Pubmed]
  4. Lysine N(zeta)-Decarboxylation in the BlaR1 Protein from Staphylococcus aureus at the Root of Its Function As an Antibiotic Sensor. Cha, J., Mobashery, S. J. Am. Chem. Soc. (2007) [Pubmed]
  5. Crystal structure of the sensor domain of the BlaR penicillin receptor from Bacillus licheniformis. Kerff, F., Charlier, P., Colombo, M.L., Sauvage, E., Brans, A., Frère, J.M., Joris, B., Fonzé, E. Biochemistry (2003) [Pubmed]
  6. Regulation of beta-lactamase synthesis as a novel site of action for suppression of methicillin resistance in Staphylococcus aureus. Bruns, O., Bruns, W., Pulverer, G. Zentralbl. Bakteriol. (1997) [Pubmed]
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