Reference : A lysine cluster in domain II of Bacillus subtilis PBP4a plays a role in the membrane...
Scientific congresses and symposiums : Poster
Life sciences : Microbiology
http://hdl.handle.net/2268/184011
A lysine cluster in domain II of Bacillus subtilis PBP4a plays a role in the membrane attachment of this C1 PBP.
English
[fr] Un groupe de lysines en surface du domaine II du PBP4a de Bacillus subtilis joue un rôle dans l'attachement de ce PBP C1 à la membrane
Vanden Broeck, Arnaud mailto [Université de Liège - ULg > Centre of Protein Engineering > > >]
Dauvin, Marjorie mailto [Université de Liège > Département des sciences de la vie > Physiologie et génétique bactériennes >]
Sauvage, Eric mailto [Université de Liège - ULg > Cristallographie > Centre of Protein Engineering > >]
Duez, Colette mailto [Université de Liège > > Centre d'ingénierie des protéines >]
8-Jun-2015
A0
No
Yes
International
IAP annual meeting iPRos project
June 8 2015
ULg Centre of Protein Engineering
Liège
Belgium
[en] Penicillin-binding Protein (PBP) ; class-C1 LMM PBP
[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: K86, K114, K119 and K265 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). After purification, their binding to B. subtilis membranes has been compared: WT PBP4a interacts in vitro with membranes isolated from this organism in contrast to Mut4KQ PBP4a that remains entirely unbound. In absence of any amphiphilic peptide in PBP4a, the crown of positive charges on the surface of domain II is likely responsible for the PBP cellular localization in interaction with the cytoplasmic membrane.
Centre of Protein engineering ULg
Belgian science Policy (Belspo) IAP P6/19 and P7/44
iPros: Integrative Protein science: from small molecules to complex biological systems
Researchers ; Professionals ; Students
http://hdl.handle.net/2268/184011

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