ORBi: Joris Bernard - Expression in Escherichia Coli of the Carboxy Terminal Domain of the Blar Sensory-Transducer Protein of Bacillus Licheniformis as a Water-Soluble Mr 26,000 Penicillin-Binding Protein

Reference : Expression in Escherichia Coli of the Carboxy Terminal Domain of the Blar Sensory-Transd...


	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Biochemistry, biophysics & molecular biology
	To cite this reference:	http://hdl.handle.net/2268/91657

Title :	Expression in Escherichia Coli of the Carboxy Terminal Domain of the Blar Sensory-Transducer Protein of Bacillus Licheniformis as a Water-Soluble Mr 26,000 Penicillin-Binding Protein
Language :	English
Author, co-author :	Joris, Bernard [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
	Ledent, P. [Université de Liège - ULg > > Centre d'ingénierie des protéines > > > >]
	Kobayashi, T. [Waksman Institute of Microbiology > > > >]
	Lampen, J.-O. [Waksman Institute of Microbiology > > > >]
	Ghuysen, Jean-Marie [Université de Liège - ULg > > Centre d'ingénierie des protéines > > > >]
Publication date :	15-Jun-1990
Journal title :	FEMS Microbiology Letters
Publisher :	Blackwell Publishing
Volume :	58
Issue/season :	1
Pages :	107-113
Audience :	International
ISSN :	0378-1097
e-ISSN :	1574-6968
City :	Oxford
Country :	United Kingdom
Keywords :	[en] beta-lactamase induction ; Escherichia coli ; Bacillus Licheniformis ; BLAR-CTD
Abstract :	[en] A cloning vector has been constructed which allows production and export by Escherichia coli of the Met346-Arg601 carboxy terminal domain of the 601 amino acid BLAR sensory-transducer involved in beta-lactamase inducibility in Bacillus licheniformis. The polypeptide, referred to as BLAR-CTD, accumulates in the periplasm of E. coli in the form of a water-soluble, Mr 26,000 penicillin-binding protein. These data and homology searches suggest that BLAR has a membrane topology similar to that of other sensory-transducers involved in chemotaxis.
Funders :	Fonds de la Recherche Scientifique Médicale - FRSM ; Fond de la Recherche de la Faculté de Médecine ULg ; National Institutes for Allergy and Infectious Deseases
Target :	Researchers ; Professionals
Permalink :	http://hdl.handle.net/2268/91657

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