Reference : The Enterococcus Hirae R40 Penicillin-Binding Protein 5 and the Methicillin-Resistant...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/81165
The Enterococcus Hirae R40 Penicillin-Binding Protein 5 and the Methicillin-Resistant Staphylococcus Aureus Penicillin-Binding Protein 2' Are Similar
English
el Kharroubi, Aboubaker [Université de Liège - ULiège > Institut de Chimie > Centre d'Ingénierie des Protéines > > >]
Jacques, Philippe mailto [Université de Liège - ULiège > Institut de Chimie > Centre d'Ingénierie des Protéines > > >]
Piras, Graziella [Université de Liège - ULiège > Institut de Chimie > Centre d'Ingénierie des Protéines > > >]
Van Beeumen, Jozef [Rijksuniversiteit-Gent > > Laboratorium voor Microbiologie en Microbiële Genetica > > >]
Coyette, Jacques [Rijksuniversiteit-Gent > > Laboratorium voor Microbiologie en Microbiele Genetica > >]
Ghuysen, Jean-Marie [Université de Liège - ULiège > Institut de Chimie > Centre d'Ingénierie des Protéines > > >]
1-Dec-1991
Biochemical Journal
Portland Press
280
Pt 2
463-469
Yes (verified by ORBi)
International
0264-6021
1470-8728
London
United Kingdom
[en] Penicillin binding protein ; Nucleotide sequence ; Aminoacid sequence ; Polymerase chain reaction ; Enterococcus ; Staphylococcus aureus ; Streptococcaceae ; Micrococcales ; Micrococcaceae
[fr] Protéine liaison pénicilline ; Séquence nucléotide ; Séquence aminoacide ; Réaction chaîne polymérase ; Enterococcus ; Staphylococcus aureus
[en] Enterococcus hirae ; Streptococcaceae ; Micrococcales
[en] The penicillin-resistant Enterococcus hirae R40 has a typical profile of membrane-bound penicillin-binding proteins (PBPs) except that the 71 kDa PBP5 of low penicillin affinity represents about 50% of all the PBPs present. Water-soluble tryptic-digest peptides were selectively produced from PBP5, their N-terminal regions were sequenced and synthetic oligonucleotides were used as primers to generate a 476 bp DNA fragment by polymerase chain reaction. On the basis of these data, the PBP5-encoding gene was cloned in Escherichia coli by using pBR322 as vector. The gene, included in a 7.1 kb insert, had the information for a 678-amino acid-residue protein. PBP5 shows similarity, in the primary structure, with the high-molecular-mass PBPs of class B. In particular, amino acid alignment of the enterococcal PBP5 and the methicillin-resistant staphylococcal PBP2' generates scores that are 30, for the N-terminal domains, and 53, for the C-terminal domains, standard deviations above that expected for a run of 20 randomized pairs of proteins having the same amino acid compositions as the two proteins under consideration.
Centre d'Ingénierie des Protéines - CIP
Fonds de la Recherche Scientifique (Communauté française de Belgique) - F.R.S.-FNRS ; Fonds de la Recherche Scientifique Médicale - FRSM
Researchers ; Professionals ; Students
http://hdl.handle.net/2268/81165

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