Reference : The Penicillin sensory transducer, blar, involved in the inducibility of beta-lactamase ...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/64253
The Penicillin sensory transducer, blar, involved in the inducibility of beta-lactamase synthesis in bacillus licheniformis is embedded in the plasma membrane via a four-alpha-helix bundle
English
Hardt, Karin [Université de Liège - ULg > > Centre d'ingéniérie des protéines > >]
Joris, Bernard mailto [Université de Liège > > Physiologie et génétique bactériennes >]
Lepage, Sophie [Université de Liège - ULg > Institut de Chimie > Centre d'ingénierie des Protéines > >]
Brasseur, Robert mailto [Université de Liège - ULg > > Gembloux Agro-Bio Tech > > >]
Lampen, J. Olivier [State University of New Jersey > Waksman Institute > > >]
Frère, Jean-Marie mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines > > >]
Fink, Anthony L. [University of California > Department of Chemistry and Biochemistry > > >]
Ghuysen, Jean-Marie [Université de Liège - ULg > > Centre d'ingénierie des protéines > > >]
1997
Molecular Microbiology
Blackwell Publishing
23
5
935-944
Yes (verified by ORBi)
International
0950-382X
1365-2958
Oxford
United Kingdom
[en] Prediction studies, conformational analyses and membrane-topology mapping lead to the conclusion that the penicillin sensory transducer, BlaR, involved in the inducibility of beta-lactamase synthesis in Bacillus licheniformis, is embedded in the plasma membrane bilayer via four transmembrane segments TM1-TM4 that forma four-alpha-helix bundle. The extracellular 262-amino-acid-residue polypeptide, S340-R601, that is fused at the carboxy end of TM4, possesses the amino acid sequence signature of a penicilloyl serine transferase. It probably functions as penicillin sensor. As an independent entity, this polypeptide behaves as a high-affinity penicillin-binding protein. As a component of the full-size BlaR, it adopts a different conformation presumably because of interactions with the extracellular 63-amino-acid-residue P53-S115 loop that connects TM2 and TM3.
Reception of the penicillin-induced signal requires a precise conformation of the sensor but it does not involve penicilloylation of the serine residue S402 of motif STYK. Signal transmission through the plasma membrane by the four-alpha-helix bundle may proceed in a way comparable to that of the aspartate receptor, Tar. Signal emission in the cytosol by the intracellular 189-amino-acid-residue Y134-K322 loop that connects TM3 and TM4, may proceed via the activation of a putative metallopeptidase.
Centre d'Ingénierie des Protéines - CIP
Fonds de la Recherche Fondamentale Collective - FRFC ; Fonds de la Recherche Scientifique (Communauté française de Belgique) - F.R.S.-FNRS
Researchers ; Professionals
http://hdl.handle.net/2268/64253
The definitive version is available at www.blackwell-synergy.com

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