References of "Joris, Bernard"
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See detailRegulation Of The Beta-Lactamase Blal Of Streptomyces-Cacaoi - The Product Of The Blab Regulatory Gene Is An Internal Membrane-Bound Protein
Magdalena, J.; Joris, Bernard ULg; Vanbeeumen, J. et al

in Biochemical Journal (1995), 311

The beta-lactamase-encoding gene blaL, cloned from Streptomyces cacaoi in Streptomyces lividans, is inducible by beta-lactam compounds. This regulation has been shown to depend on the products of two open ... [more ▼]

The beta-lactamase-encoding gene blaL, cloned from Streptomyces cacaoi in Streptomyces lividans, is inducible by beta-lactam compounds. This regulation has been shown to depend on the products of two open reading frames, ORF1 (blaA) and ORF2 (blaB) [Lenzini, Magdalena, Fraipont, Joris, Matagne and Dusart (1992) Mol. Gen. Genet. 235, 41-48]. BlaA belongs to the LysR family of transcription activators, whereas BlaB shares some features with the penicillin-recognizing proteins. BlaB has now been overexpressed in Escherichia coli, purified and used for antibody preparation. Immunoblotting of cell-fractionated materials from S. cacaoi showed that BlaB is attached to the internal face of the cytoplasmic membrane. It could not be released by high salt concentrations or EDTA, but only by protease treatment. Under the assay conditions, BlaB did not act as a penicillin-binding protein, a beta-lactamase, a D-amino-peptidase or a target in a phosphorylation step. [less ▲]

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See detailAnalysis of the open reading frames of the main capsid proteins of actinophage VWB.
Anne, J; Fiten, P; Van Mellaert, L et al

in Archives of Virology (1995), 140(6), 1033-47

The nucleotide sequence of a 6 kb fragment encoding the main late proteins (p14, p38 and p24) of actinophage VWB was obtained. Sequence comparison of the encoded proteins with those filed in databases ... [more ▼]

The nucleotide sequence of a 6 kb fragment encoding the main late proteins (p14, p38 and p24) of actinophage VWB was obtained. Sequence comparison of the encoded proteins with those filed in databases indicated that the phage VWB main late proteins were all novel. A search for special motifs revealed that p14 (13.3 kDa) has a P-loop sequence commonly found in ATP- and GTP-binding proteins. This observation might indicate that p14 is important for ATP-driven DNA translocation during encapsidation of VWB phage DNA into the phage head. Furthermore, the polypeptide ORF2 (26.9 kDa) has an unusual primary structure consisting of 3 stretches of acidic amino acid residues and a glycine/arginine rich C-terminal end. From comparison with other proteins including the bacteriophage T4 prohead core component and from the data of special motif analysis the ORF2 gene product is probably involved in prohead core formation. [less ▲]

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See detailKinetic properties of the Bacillus licheniformis Penicillin-binding proteins
Lepage, Sophie; Galleni, Moreno ULg; Lakaye, Bernard ULg et al

in Biochemical Journal (1995), 309

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See detailErratum for : primary structure of the streptomyces R61 extracellular DD-peptidase. 1. Cloning into Streptomyces lividans and nucleotide sequence of the gene
Duez, Colette ULg; Piron-Fraipont, C.; Joris, Bernard ULg et al

in European Journal of Biochemistry (1994), 224(3), 1079

This is the correction of the fig. 5 of Primary structure of the Streptomyces R61 extracellular DD-peptidase. 1. Cloning into Streptomyces Zividuns and nucleotide sequence of the gene, by C. Duez, C ... [more ▼]

This is the correction of the fig. 5 of Primary structure of the Streptomyces R61 extracellular DD-peptidase. 1. Cloning into Streptomyces Zividuns and nucleotide sequence of the gene, by C. Duez, C. Piron-Fraipont, B. Joris, J. Dusart, M. S. Urdea, J. A. Martial, J.-M. Frère and J.-M. Ghuysen. European Journal of Biochemistry Volume 162, Issue 3, pages 509–518, February 1987 [less ▲]

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See detailThe Precursor of the Streptomyces R61 Dd-Peptidase Containing a C-Terminal Extension Is Inactive
Fanuel, Laurence; Granier, Benoît; Wilkin, Jean-Marc et al

in FEBS Letters (1994), 351(1), 49-52

The Streptomyces R61 DD-peptidase gene encodes a 26-residue C-terminal extension which is not found in the mature protein. When the gene was expressed in Escherichia coli, the extension was not cleaved ... [more ▼]

The Streptomyces R61 DD-peptidase gene encodes a 26-residue C-terminal extension which is not found in the mature protein. When the gene was expressed in Escherichia coli, the extension was not cleaved and the precursor protein was not enzymatically active. It also reacted with penicillins significantly more slowly than the mature protein. The introduction of a 'stop' codon after that corresponding to the C-terminal residue of the mature protein resulted in the production of an active protein in the periplasm of E. coli. [less ▲]

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See detailBinding Site-Shaped Repeated Sequences of Bacterial Wall Peptidoglycan Hydrolases
Ghuysen, Jean-Marie ULg; Lamotte-Brasseur, Josette; Joris, Bernard ULg et al

in FEBS Letters (1994), 342(1), 23-28

The non-catalytic C-terminal regions of the N-acetylmuramidase (lysozyme) of Clostridium acetobutylicum and N-acetylmuramoyl(D-lactyl)-L-alanine amidases CwlA of Bacillus subtilis, ORFL3 and CwlL of ... [more ▼]

The non-catalytic C-terminal regions of the N-acetylmuramidase (lysozyme) of Clostridium acetobutylicum and N-acetylmuramoyl(D-lactyl)-L-alanine amidases CwlA of Bacillus subtilis, ORFL3 and CwlL of Bacillus licheniformis were previously reported to have similarities with the amino acid sequence of the non-catalytic N-terminal module of the Streptomyces albus G Zn DD-peptidase. This peptidase is a bipartite protein of known three-dimensional structure. Its non-catalytic N-terminal module possesses, exposed at the surface, an elongated crevice which is defined by a loop-helix-loop-helix motif that consists of two repeats, each 16 amino acid residues long, connected by a heptapeptide and whose design is compatible with its possible functioning as a substrate recognition and binding site. Amino acid alignments suggest that cavities nearly identical in shape to that present in the non-catalytic module of the S. albus peptidase, are borne by the C-terminal regions of the CwlA amidase (in one copy), the lysozyme and the ORFL3 and CwlL amidases (in two copies). Since a common feature of the five enzymes is their substrate, the bacterial cell wall peptidoglycan, we interpret the striking similarity of their non-catalytic N- or C-terminal modules to suggest that these modules are involved in the binding of these exocellular enzymes to their insoluble wall substrate. [less ▲]

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See detailSerine-Type D-Ala-D-Ala Peptidases and Penicillin-Binding Proteins
Granier, Benoît; Jamin, Marc; Adam, Maggy et al

in Methods in Enzymology (1994), 244

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See detailThe mechanism of action of DD-peptidases: the role of Threonine-299 and -301 in the Streptomyces R61 DD-peptidase.
Wilkin, J M; Dubus, Alice ULg; Joris, Bernard ULg et al

in Biochemical Journal (1994), 301 ( Pt 2)

The side chains of residues Thr299 and Thr301 in the Streptomyces R61 DD-peptidase have been modified by site-directed mutagenesis. These amino acids are part of a beta-strand which forms a wall of the ... [more ▼]

The side chains of residues Thr299 and Thr301 in the Streptomyces R61 DD-peptidase have been modified by site-directed mutagenesis. These amino acids are part of a beta-strand which forms a wall of the active-site cavity. Thr299 corresponds to the second residue of the Lys-Thr(Ser)-Gly triad, highly conserved in active-site beta-lactamases and penicillin-binding proteins (PBPs). Modification of Thr301 resulted only in minor alterations of the catalytic and penicillin-binding properties of the enzyme. No selective decrease of the rate of acylation was observed for any particular class of compounds. By contrast, the loss of the hydroxy group of the residue in position 299 yielded a seriously impaired enzyme. The rates of inactivation by penicillins were decreased 30-50-fold, whereas the reactions with cephalosporins were even more affected. The efficiency of hydrolysis against the peptide substrate was also seriously decreased. More surprisingly, the mutant was completely unable to catalyse transpeptidation reactions. The conservation of an hydroxylated residue in this position in PBPs is thus easily explained by these results. [less ▲]

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See detailTranscription and expression analysis, using lacZ and phoA gene fusions, of Mycobacterium fortuitum beta-lactamase genes cloned from a natural isolate and a high-level beta-lactamase producer.
Timm, J; Perilli, M G; Duez, Colette ULg et al

in Molecular Microbiology (1994), 12(3), 491-504

The gene encoding a class A beta-lactamase was cloned from a natural isolate of Mycobacterium fortuitum (blaF) and from a high-level amoxicillin-resistant mutant that produces large amounts of beta ... [more ▼]

The gene encoding a class A beta-lactamase was cloned from a natural isolate of Mycobacterium fortuitum (blaF) and from a high-level amoxicillin-resistant mutant that produces large amounts of beta-lactamase (blaF*). The nucleotide sequences of the two genes differ at 11 positions, including two in the region upstream from the coding sequence. Gene fusions to Escherichia coli lacZ and transcription and expression analysis of the cloned genes in Mycobacterium smegmatis indicated that high-level production of the beta-lactamase in the mutant is mainly or wholly due to a single base pair difference in the promoter. These analyses also showed that transcription and translation start at the same position. A comparison of the amino acid sequence of BlaF, as predicted from the nucleotide sequence, with the determined N-terminal amino acid sequence indicated the presence of a typical signal peptide. The fusion of blaF (or blaF*) to the E. coli gene phoA resulted in the production of BlaF-PhoA hybrid proteins that had alkaline phosphatase activity. These results demonstrate that phoA can be used as a reporter gene for studying protein export in mycobacteria. [less ▲]

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See detailAnalysis of the penA gene of Pseudomonas cepacia 249.
Joris, Bernard ULg; Galleni, Moreno ULg; Frère, Jean-Marie ULg et al

in Antimicrobial Agents and Chemotherapy (1994), 38(2), 407-8

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See detailA common system controls the induction of very different genes. The class-A beta-lactamase of Proteus vulgaris and the enterobacterial class-C beta-lactamase.
Datz, M; Joris, Bernard ULg; Azab, E A et al

in European Journal of Biochemistry (1994), 226(1), 149-57

Among the Enterobacteriaceae, Proteus vulgaris is exceptional in the inducible production of a 29-kDa beta-lactamase (cefuroximase) with an unusually high activity towards the beta-lactamase-stable ... [more ▼]

Among the Enterobacteriaceae, Proteus vulgaris is exceptional in the inducible production of a 29-kDa beta-lactamase (cefuroximase) with an unusually high activity towards the beta-lactamase-stable oximino-cephalosporins (e.g. cefuroxime and cefotaxime). Sequencing of the corresponding gene, cumA, showed that the derived CumA beta-lactamase belonged to the molecular class A. The structural gene was under the direct control of gene cumR, which was transcribed backwards and whose initiation codon was 165 bp away from that of the beta-lactamase gene. This resembled the arrangement of structural and regulator genes ampC and ampR of the 39-kDa molecular-class-C beta-lactamase AmpC present in many enterobacteria. Moreover, cloned genes ampD and ampG for negative modulation and signal transduction of AmpC beta-lactamase induction, respectively, were also able to restore constitutively CumA overproducing and non-inducible P. vulgaris mutants to the inducible, wild-type phenotype. The results indicate that controls of the induction phenomena are equivalent for the CumA and AmpC beta-lactamase. Very different structural genes can thus be under the control of identical systems. [less ▲]

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See detailSynthesis, purification and kinetic properties of fluorescein-labelled penicillins
Lakaye, Bernard ULg; Damblon, Christian ULg; Jamin, Marc et al

in Biochemical Journal (1994), 300

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See detailModular Design of the Bi(multi?) functional penicillin-binding proteins
Englebert, Serge; El Kharroubi, Aboubaker; Piras, Graziella et al

in De pedro; Höltje, J. V.; Loffelhardt, W. (Eds.) Bacterial Growth & Lysis Metabolism and Structure of the Bacterial Sacculus (1993)

Proceedings of a symposium held in Mallorca, Spain in April 1992. The goal of the meeting was to assess the present state of knowledge on the structure and physiology of the bacterium murien sacculus, and ... [more ▼]

Proceedings of a symposium held in Mallorca, Spain in April 1992. The goal of the meeting was to assess the present state of knowledge on the structure and physiology of the bacterium murien sacculus, and develop new hypotheses and strategies to promote further development of the field. The contributions reflect broadly different approaches. Papers discuss structure and chemistry, biosynthesis and maturation, regulation and control of cell wall hydrolases, penicillin interactive proteins, morphogenesis and septum formation, and cell growth. Annotation c. Book News, Inc., Portland, OR (booknews.com) [less ▲]

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See detailCharacterization of the Sporulation-Related Gamma-D-Glutamyl-(L)Meso-Diaminopimelic-Acid-Hydrolysing Peptidase I of Bacillus Sphaericus NCTC 9602 as a Member of the Metallo(Zinc) Carboxypeptidase A Family. Modular Design of the Protein
Hourdou, Marie-Laure; Guinand, Micheline; Vacheron, Marie-Jeanne et al

in Biochemical Journal (1993), 292(Pt 2), 563-570

The sporulation-related gamma-D-glutamyl-(L)meso-diaminopimelic-acid-hydrolysing peptidase I of Bacillus sphaericus NCTC 9602 has been analysed by proton-induced X-ray emission. It contains 1 equivalent ... [more ▼]

The sporulation-related gamma-D-glutamyl-(L)meso-diaminopimelic-acid-hydrolysing peptidase I of Bacillus sphaericus NCTC 9602 has been analysed by proton-induced X-ray emission. It contains 1 equivalent Zn2+ per mol of protein. As derived from gene cloning and sequencing, the B. sphaericus Zn peptidase I is a two-module protein. A 100-amino-acid-residue N-terminal domain consisting of two tandem segments of similar sequences, is fused to a 296-amino-acid-residue C-terminal catalytic domain. The catalytic domain belongs to the Zn carboxypeptidase A family, the closest match being observed with the Streptomyces griseus carboxypeptidase [Narahashi (1990) J. Biochem. 107, 879-886] and with the family prototype, bovine carboxypeptidase A. The catalytic domain of the B. sphaericus peptidase I possesses, distributed along the amino-acid sequence, peptide segments, a triad His162-Glu165-His307 and a dyad Tyr347-Glu366 that are equivalent to secondary structures, the zinc-binding triad His69-Glu72-His196 and the catalytic dyad Tyr248-Glu270 of bovine carboxypeptidase A respectively. The N-terminal repeats of the B. sphaericus peptidase I have similarity with the C-terminal repeats of the Enterococcus hirae muramidase 2, the Streptococcus (now Enterococcus) faecalis autolysin and the Bacillus phi PZA and phi 29 lysozymes, to which a role in the recognition of a particular moiety of the bacterial cell envelope has been tentatively assigned. Detergents enhance considerably the specific activity of the B. sphaericus peptidase I. [less ▲]

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See detailThe Mechanism of Action of DD-Peptidases: The Role of Tyrosine-159 in the Streptomyces R61 DD-Peptidase
Wilkin, Jean-Marc; Jamin, Marc; Damblon, Christian ULg et al

in Biochemical Journal (1993), 291(Part 2), 537-544

Tyrosine-159 of the Streptomyces R61 penicillin-sensitive DD-peptidase was replaced by serine or phenylalanine. The second mutation yielded a very poorly active protein whose rate of penicillin binding ... [more ▼]

Tyrosine-159 of the Streptomyces R61 penicillin-sensitive DD-peptidase was replaced by serine or phenylalanine. The second mutation yielded a very poorly active protein whose rate of penicillin binding was also drastically decreased, except for the reactions with nitrocefin and methicillin. The consequences of the first mutation were more surprising, since a large proportion of the thiolesterase activity was retained, together with the penicillin-binding capacity. Conversely, the peptidase properties was severely affected. In both cases, a drastic decrease in the transferase activity was observed. The results are compared with those obtained by mutation of the corresponding residue in the class A beta-lactamase of Streptomyces albus G. [less ▲]

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See detailA New, Highly Sensitive Method for the Detection and Quantification of Penicillin-Binding Proteins
Galleni, Moreno ULg; Lakaye, Bernard ULg; Lepage, Sophie et al

in Biochemical Journal (1993), 291((Pt 1)), 19-21

A new method for the identification and quantification of penicillin-binding proteins is described which uses fluorescein-coupled penicillins. It allows the rapid detection of 0.2 pmol with the naked eye ... [more ▼]

A new method for the identification and quantification of penicillin-binding proteins is described which uses fluorescein-coupled penicillins. It allows the rapid detection of 0.2 pmol with the naked eye and 2 fmol with the help of an A.L.F. automatic DNA sequencer. Direct labelling can also be performed on whole bacterial cells. [less ▲]

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See detailSequence of a gene encoding a (poly ManA) alginate lyase active on Pseudomonas aeruginosa alginate
Malissard, Martine; Duez, Colette ULg; Guinand, Micheline et al

in FEMS Microbiology Letters (1993), 110(1), 101-106

The recombinant plasmid pAL-A3 bears a (poly ManA) alginate lyase-encoding gene that originates from the marine bacterium ATCC 433367 (Brown et al., Appl. Environ. Microbiol. (1991) 57, 1870-1872). The ... [more ▼]

The recombinant plasmid pAL-A3 bears a (poly ManA) alginate lyase-encoding gene that originates from the marine bacterium ATCC 433367 (Brown et al., Appl. Environ. Microbiol. (1991) 57, 1870-1872). The alginate lyase produced by Escherichia coli TC4 harbouring pAL-A3 was purified to protein homogeneity and the corresponding gene sequenced, giving access to the first known primary structure of an alginate lyase. The 265-amino acid residue alginate lyase showed lytic activity on a Pseudomonas aeruginosa alginate isolated from a cystic fibrosis patient. Unexpectedly, the alginate lyase thus characterized differed from that isolated from the culture medium of the bacterium ATCC 433367 (Romeo and Preston, Biochemistry (1986) 25, 8385-8391). [less ▲]

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See detailMechanism of action of DD-peptidases: role of asparagine-161 in the Streptomyces R61 DD-peptidase.
Wilkin, J M; Jamin, M; Joris, Bernard ULg et al

in Biochemical Journal (1993), 293 ( Pt 1)

The role of residue Asn-161 in the interaction between the Streptomyces R61 DD-peptidase and various substrates or beta-lactam inactivators was probed by site-directed mutagenesis. The residue was ... [more ▼]

The role of residue Asn-161 in the interaction between the Streptomyces R61 DD-peptidase and various substrates or beta-lactam inactivators was probed by site-directed mutagenesis. The residue was successively replaced by serine and alanine. In the first case, acylation rates were mainly affected with the peptide and ester substrates but not with the thiol-ester substrates and beta-lactams. However, the deacylation rates were decreased 10-30-fold with the substrates yielding benzoylglycyl and benzoylalanyl adducts. The Asn161Ala mutant was more generally affected, although the acylation rates with cefuroxime and cefotaxime remained similar to those observed with the wild-type enzyme. Surprisingly, the deacylation rates of the benzoylglycyl and benzoylalanyl adducts were very close to those observed with the wild-type enzyme. The results also indicate that the interaction with the peptide substrate and the transpeptidation reaction were more sensitive to the mutations than the other reactions studied. The results are discussed and compared with those obtained with the Asn-132 mutants of a class A beta-lactamase. [less ▲]

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See detailA comparative study of class-D beta-lactamases.
Ledent, Philippe; Raquet, X; Joris, Bernard ULg et al

in Biochemical Journal (1993), 292 ( Pt 2)

Three class-D beta-lactamases (OXA2, OXA1 and PSE2) were produced and purified to protein homogeneity. 6 beta-Iodopenicillanate inactivated the OXA2 enzyme without detectable turnover. Labelling of the ... [more ▼]

Three class-D beta-lactamases (OXA2, OXA1 and PSE2) were produced and purified to protein homogeneity. 6 beta-Iodopenicillanate inactivated the OXA2 enzyme without detectable turnover. Labelling of the same beta-lactamase with 6 beta-iodo[3H]penicillanate allowed the identification of Ser-70 as the active-site serine residue. In agreement with previous reports, the apparent M(r) of the OXA2 enzyme as determined by molecular-sieve filtration, was significantly higher than that deduced from the gene sequence, but this was not due to an equilibrium between a monomer and a dimer. The heterogeneity of the OXA2 beta-lactamase on ion-exchange chromatography contrasted with the similarity of the catalytic properties of the various forms. A first overview of the enzymic properties of the three 'oxacillinases' is presented. With the OXA2 enzyme, 'burst' kinetics, implying branched pathways, seemed to prevail with many substrates. [less ▲]

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See detailAn overview of the kinetic parameters of class B beta-lactamases.
Felici, A; Amicosante, G; Oratore, A et al

in Biochemical Journal (1993), 291 ( Pt 1)

The catalytic properties of three class B beta-lactamases (from Pseudomonas maltophilia, Aeromonas hydrophila and Bacillus cereus) were studied and compared with those of the Bacteroides fragilis enzyme ... [more ▼]

The catalytic properties of three class B beta-lactamases (from Pseudomonas maltophilia, Aeromonas hydrophila and Bacillus cereus) were studied and compared with those of the Bacteroides fragilis enzyme. The A. hydrophila beta-lactamase exhibited a unique specificity profile and could be considered as a rather specific 'carbapenemase'. No relationships were found between sequence similarities and catalytic properties. The problem of the repartition of class B beta-lactamases into sub-classes is discussed. Improved purification methods were devised for the P. maltophilia and A. hydrophila beta-lactamases including, for the latter enzyme, a very efficient affinity chromatography step on a Zn(2+)-chelate column. [less ▲]

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