Reference : Studies of the Domains II and III of Bacillus subtilis PBP4a in relation with the pro...
Scientific congresses and symposiums : Poster
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/166421
Studies of the Domains II and III of Bacillus subtilis PBP4a in relation with the protein localization
English
Vanden Broeck, Arnaud mailto [Université de Liège - ULiège > > > 2e an. master bioch. & biol. moléc. & cell., fin. appr.]
Van Der Heiden, Edwige mailto [Université de Liège - ULiège > > Centre d'ingénierie des protéines >]
Sauvage, Eric mailto [Université de Liège - ULiège > > Centre d'ingénierie des protéines >]
Rhazi, Noureddine [> >]
Huynen, Céline mailto [Université de Liège - ULiège > Département des sciences de la vie > Enzymologie et repliement des protéines >]
Verlaine, Olivier mailto [Université de Liège - ULiège > > Centre d'ingénierie des protéines >]
Joris, Bernard mailto [Université de Liège - ULiège > Département des sciences de la vie > Physiologie et génétique bactériennes >]
Duez, Colette mailto [Université de Liège - ULiège > > Centre d'ingénierie des protéines >]
23-Apr-2014
A0
No
No
National
IAP Day - iPROS
23rd of April 2014
uGhent
Ghent
Belgium
[en] Bacillus ; PBP ; Cellular localization
[en] Bacillus subtilis PBP4a belongs to the class-C1 PBPs characterized by two internal additional domains of unknown function. Seven lysine residues (K) are protruding from domain II. Four of them have been mutated in glutamine residues (Q). Both proteins (WT and Mut4KQ PBP4a) have been produced without signal peptide in E. coli and their sub-cellular localizations determined by measuring the DD-carboxypeptidase activities in the different compartments (cytoplasmic vs membrane attached proteins). In order to detect a possible influence of the PBP4a domain III in the localization of the protein, its encoding sequence has been cloned into pET-28b-BlaP, a vector allowing the production of WT BlaP β-lactamase or BlaP/DIII chimeric protein (with domain III inserted in a permissive loop of BlaP). The nitrocefin hydrolysis activities of BlaP or BlaP/DIII have been measured in the different cellular compartments.
Centre for Protein Engineering
Belgian Science Policy : IAP n° P6/19 and P7/44
Researchers ; Professionals
http://hdl.handle.net/2268/166421

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