References of "Joris, Bernard"
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See detailUse of an Automatic DNA Sequencer for S1 Mapping: Transcriptional Analysis of the Streptomyces Coelicolor A3(2) Dnak Operon
Brans, Alain ULg; Loriaux, Axelle; Thamm, Iris ULg et al

in FEMS Microbiology Letters (1997), 149(2), 189-94

The transcription start point of the dnaK operon of Streptomyces coelicolor A3(2) has been determined by S1 mapping, using the EMBL automated fluorescent DNA sequencer. The -35 and -10 hexamers correspond ... [more ▼]

The transcription start point of the dnaK operon of Streptomyces coelicolor A3(2) has been determined by S1 mapping, using the EMBL automated fluorescent DNA sequencer. The -35 and -10 hexamers correspond to a sigma 70-type promoter. This promoter responds to heat shock and involves an inverted repeat different from the CIRCE sequence characteristic of the Gram-positive heat-shock promoters. [less ▲]

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See detailPenicillin-binding proteins. Wall peptidoglycan assembly and resistance to penicillin: facts, doubts and hopes
Ghuysen, Jean-Marie ULg; Charlier, Paulette ULg; Coyette, Jacques ULg et al

in International Journal of Antimicrobial Agents (1997), 8(1), 45-60

As the protein sequence and structure databases expand, the relationships between proteins, the notion of protein superfamily, and the driving forces of evolution are better understood. Key steps of the ... [more ▼]

As the protein sequence and structure databases expand, the relationships between proteins, the notion of protein superfamily, and the driving forces of evolution are better understood. Key steps of the synthesis of the bacterial cell wall peptidoglycan are revisited in light of these advances. The reactions through which the D-alanyl-D-alanine depeptide is formed, utilized, and hydrolyzed and the sites of action of the glycopeptide and β-lactam antibiotics illustrate the concept according to which new enzyme functions evolve as a result of tinkering of existing proteins. This occurs by the acquisition of local structural changes, the fusion into mul-timodular polypeptides, and the association into multiprotein complexes. [less ▲]

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See detailThe Complete Genome Sequence Of The Gram-Positive Bacterium Bacillus Subtilis
Kunst, F.; Ogasawara, N.; Moszer, I. et al

in Nature (1997), 390(6657), 249-256

Bacillus subtilis is the best-characterized member of the Gram-positive bacteria. Its genome of 4,214,810 base pairs comprises 4,100 protein-coding genes. Of these protein-coding genes, 53% are ... [more ▼]

Bacillus subtilis is the best-characterized member of the Gram-positive bacteria. Its genome of 4,214,810 base pairs comprises 4,100 protein-coding genes. Of these protein-coding genes, 53% are represented once, while a quarter of the genome corresponds to several gene families that have been greatly expanded by gene duplication, the largest family containing 77 putative ATP-binding transport proteins. In addition, a large proportion of the genetic capacity is devoted to the utilization of a variety of carbon sources, including many plant-derived molecules. The identification of five signal peptidase genes, as well as several genes for components of the secretion apparatus, is important given the capacity of Bacillus strains to secrete large amounts of industrially important enzymes. Many of the genes are involved in the synthesis of secondary metabolites, including antibiotics, that are more typically associated with Streptomyces species. The genome contains at least ten prophages or remnants of prophages, indicating that bacteriophage infection has played an important evolutionary role in horizontal gene transfer, in particular in the propagation of bacterial pathogenesis. [less ▲]

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See detailSite-directed mutagenesis of glutamate 166 in two beta-lactamases. Kinetic and molecular modeling studies.
Guillaume, Gilliane; Vanhove, M; Lamotte-Brasseur, J et al

in Journal of Biological Chemistry (1997), 272(9), 5438-44

The catalytic pathway of class A beta-lactamases involves an acyl-enzyme intermediate where the substrate is ester-linked to the Ser-70 residue. Glu-166 and Lys-73 have been proposed as candidates for the ... [more ▼]

The catalytic pathway of class A beta-lactamases involves an acyl-enzyme intermediate where the substrate is ester-linked to the Ser-70 residue. Glu-166 and Lys-73 have been proposed as candidates for the role of general base in the activation of the serine OH group. The replacement of Glu-166 by an asparagine in the TEM-1 and by a histidine in the Streptomyces albus G beta-lactamases yielded enzymes forming stable acyl-enzymes with beta-lactam antibiotics. Although acylation of the modified proteins by benzylpenicillin remained relatively fast, it was significantly impaired when compared to that observed with the wild-type enzyme. Moreover, the E166N substitution resulted in a spectacular modification of the substrate profile much larger than that described for other mutations of Omega-loop residues. Molecular modeling studies indicate that the displacement of the catalytic water molecule can be related to this observation. These results confirm the crucial roles of Glu-166 and of the "catalytic" water molecule in both the acylation and the deacylation processes. [less ▲]

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See detailThe two beta-lactamase genes of Streptomyces cacaoi, blaL and blaU, are under the control of the same regulatory system.
Magdalena, J; Gérard, Christine; Joris, Bernard ULg et al

in Molecular & General Genetics [=MGG] (1997), 255(2), 187-93

The production of beta-lactamase in Streptomyces cacaoi, which contains two beta-lactamase-encoding genes, blaL and blaU, is inducible by beta-lactam compounds. The two genes have been cloned ... [more ▼]

The production of beta-lactamase in Streptomyces cacaoi, which contains two beta-lactamase-encoding genes, blaL and blaU, is inducible by beta-lactam compounds. The two genes have been cloned independently in S. lividans TK24, a beta-lactamase-negative species. The blaU clone did not respond to the presence of beta-lactams, whereas the blaL clone appeared to be inducible in S. lividans. The latter clone contains two open reading frames, blaA and blaB, located just upstream of but transcribed divergently from blaL, which were shown to be required for the production as well as the induction of BlaL. The deduced BlaA protein belongs to the LysR family of transcription regulators. In order to examine the role of BlaA in regulation, we here report on over-expression of a GST-BlaA fusion protein in Escherichia coli and its use for antibody preparation. The GST-BlaA fusion protein was partially purified and bandshift assays showed that it bound the 197-bp blaL-blaA intergenic region. The BlaA DNA binding-site was further restricted to a 30-bp sequence containing a T-N11-A motif, a characteristic of LysR-type promoters. Another T-N11-A motif upstream of the blaU gene was also shown to bind BlaA. The affinities of these two T-N11-A motifs in BlaA binding were comparable. A plasmid bearing the blaU structural gene and the blaA-blaB regulatory region was constructed and shown to confer on an S. lividans host the capacity to produce inducible beta-lactamase. It can thus be concluded that the S. cacaoi blaL and blaU genes are controlled by the same regulatory system. [less ▲]

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See detailThe Penicillin sensory transducer, blar, involved in the inducibility of beta-lactamase synthesis in bacillus licheniformis is embedded in the plasma membrane via a four-alpha-helix bundle
Hardt, Karin; Joris, Bernard ULg; Lepage, Sophie et al

in Molecular Microbiology (1997), 23(5), 935-944

Prediction studies, conformational analyses and membrane-topology mapping lead to the conclusion that the penicillin sensory transducer, BlaR, involved in the inducibility of beta-lactamase synthesis in ... [more ▼]

Prediction studies, conformational analyses and membrane-topology mapping lead to the conclusion that the penicillin sensory transducer, BlaR, involved in the inducibility of beta-lactamase synthesis in Bacillus licheniformis, is embedded in the plasma membrane bilayer via four transmembrane segments TM1-TM4 that forma four-alpha-helix bundle. The extracellular 262-amino-acid-residue polypeptide, S340-R601, that is fused at the carboxy end of TM4, possesses the amino acid sequence signature of a penicilloyl serine transferase. It probably functions as penicillin sensor. As an independent entity, this polypeptide behaves as a high-affinity penicillin-binding protein. As a component of the full-size BlaR, it adopts a different conformation presumably because of interactions with the extracellular 63-amino-acid-residue P53-S115 loop that connects TM2 and TM3. Reception of the penicillin-induced signal requires a precise conformation of the sensor but it does not involve penicilloylation of the serine residue S402 of motif STYK. Signal transmission through the plasma membrane by the four-alpha-helix bundle may proceed in a way comparable to that of the aspartate receptor, Tar. Signal emission in the cytosol by the intracellular 189-amino-acid-residue Y134-K322 loop that connects TM3 and TM4, may proceed via the activation of a putative metallopeptidase. [less ▲]

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See detailIdentification of the active gene coding for the metastasis-associated 37LRP/p40 multifunctional protein.
Clausse, Nathalie; Jackers, Pascale ULg; Jares, P. et al

in DNA & Cell Biology (1996), 15(12), 1009-23

A 37LRP/p40 polypeptide is of major interest because it is consistently up-regulated in cancer cells in correlation with their invasive and metastatic phenotype. Furthermore, this polypeptide presents ... [more ▼]

A 37LRP/p40 polypeptide is of major interest because it is consistently up-regulated in cancer cells in correlation with their invasive and metastatic phenotype. Furthermore, this polypeptide presents intriguing multifunctional properties because it has been characterized as the precursor of the metastasis-associated 67-kD laminin receptor (67LR) and as a cytoplasmic ribosomal-associated protein. The isolation of the 37LRP/p40 gene is a prerequisite for identifying the molecular mechanisms responsible for the constant up-regulation of the 67LR expression in cancer cells. To date, the active 37LRP/p40 gene has never been identified in any species due to the existence of multiple pseudogenes in most vertebrates genomes. In this study, we report for the first time the gene structure and potential regulatory sequences of the 37 LRP/p40 gene. The chicken genome was selected to undergo this characterization because it is the only known vertebrate that bears a single 37 LRP/p40 gene copy. The 37 LRP/p40 active gene is composed of 7 exons and 6 introns and bears features characteristic of a ribosomal protein gene. It does not bear a classical TATA box and it exhibits several transcription initiation sites as demonstrated by RNase protection assay and primer extension. Analysis of potential regulatory regions suggests that gene expression is driven not only by the 5' genomic region but also by the 5' untranslated and intron 1 sequences. On the basis of gene structure and extensive protein evolutionary study, we found that the carboxyterminal domain of the protein is a conserved lock-and-key structure/function domain that could be involved in the biosynthesis of the higher-molecular-weight 67-kD laminin receptor in vertebrates, whereas the central core of the protein would be responsible for the ribosome associated function. The first identification of the active 37LRP/p40 gene presented in this study is a critical step toward the isolation of the corresponding human gene and the understanding of the molecular mechanisms involved in the up-regulation of its expression during tumor invasion and metastasis. [less ▲]

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See detailA Sequence-Specific DNA-Binding Protein Interacts with the Xlnc Upstream Region of Streptomyces Sp. Strain Ec3
Giannotta, F.; Georis, J.; Moreau, A. et al

in FEMS Microbiology Letters (1996), 142(1), 91-7

The alignment of the promoter region of several Streptomyces xylanases shows three conserved sequences which could be involved in gene regulation. By electromobility shift assays these specific sequences ... [more ▼]

The alignment of the promoter region of several Streptomyces xylanases shows three conserved sequences which could be involved in gene regulation. By electromobility shift assays these specific sequences, present only in Streptomyces xylanolytic strains, were identified as protein-binding sites. The sequence required for efficient recognition by the retarding protein appeared to be a 4-bp inverted repeat: 5'-CTTT-Nx-AAAG-3'. The DNA-protein affinity was influenced by the culture conditions. [less ▲]

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See detailIdentification and overexpression in Escherichia coli of a Mycobacterium leprae gene, pon1, encoding a high-molecular-mass class A penicillin-binding protein, PBP1
Basu, Joyoti; Mahapatra, Sebabrata; Kundu, Manikuntala et al

in Journal of Bacteriology (1996), 178(6), 1707-1711

Cosmid B577, a member of the collection of ordered clones corresponding to the genome of Mycobacterium leprae, contains a gene, provisionally called pon1, that encodes an 821-amino-acid-residue high ... [more ▼]

Cosmid B577, a member of the collection of ordered clones corresponding to the genome of Mycobacterium leprae, contains a gene, provisionally called pon1, that encodes an 821-amino-acid-residue high-molecular-mass class A penicillin-binding protein, provisionally called PBP1. With similar amino acid sequences and modular designs, M. leprae PBP1 is related to Escherichia coli PBP1a and PBP1b, bienzymatic proteins with transglycosylase and transpeptidase activities. When produced in E. coli, His tag-labelled derivatives of M. leprae PBP1 adopt the correct membrane topology, with the bulk of the polypeptide chain on the surface of the plasma membrane. They defy attempts at solubilization with all the detergents tested except cetyltrimethylammonium bromide. The solubilized PBP1 derivatives can be purified by affinity chromatography on Ni2+-nitrilotriacetic acid agarose. They have low affinities for the usual penicillins and cephalosporins. [less ▲]

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See detailPenicillin and Beyond: Evolution, Protein Fold, Multimodular Polypeptides, and Multiprotein Complexes
Ghuysen, Jean-Marie ULg; Charlier, Paulette ULg; Coyette, Jacques et al

in Microbial Drug Resistance : Mechanism, Epidemiology, & Disease (1996), 2(2, Summer), 163-175

As the protein sequence and structure databases expand, the relationships between proteins, the notion of protein superfamily, and the driving forces of evolution are better understood. Key steps of the ... [more ▼]

As the protein sequence and structure databases expand, the relationships between proteins, the notion of protein superfamily, and the driving forces of evolution are better understood. Key steps of the synthesis of the bacterial cell wall peptidoglycan are revisited in light of these advances. The reactions through which the D-alanyl-D-alanine depeptide is formed, utilized, and hydrolyzed and the sites of action of the glycopeptide and beta-lactam antibiotics illustrate the concept according to which new enzyme functions evolve as a result of tinkering of existing proteins. This occurs by the acquisition of local structural changes, the fusion into multimodular polypeptides, and the association into multiprotein complexes. [less ▲]

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See detailSelection of hammerhead ribozymes for optimum cleavage of interleukin 6 mRNA.
Hendrix, Chris; Anne, J; Joris, Bernard ULg et al

in Biochemical Journal (1996), 314 ( Pt 2)

Four GUC triplets in the coding region of the MRNA of interleukin 6 (IL-6) were examined for their suitabilty to serve as a target for hammerhead ribozome-mediated cleavage. This selection procedure was ... [more ▼]

Four GUC triplets in the coding region of the MRNA of interleukin 6 (IL-6) were examined for their suitabilty to serve as a target for hammerhead ribozome-mediated cleavage. This selection procedure was performed with the intention to downregulate IL-6 production as a potential treatment of those diseases in which IL-6 overexpression is involved. Hammerhead ribozymes and their respective short synthetic substrates (19-mers) were synthesized for these four GUC triplets. Notwithstanding the identical catalytic core sequences, the difference in base composition of the helices involved in substrate binding caused substantial variation in cleavage activity. The cleavage reactions on the 1035 nucleotide IL-6 mRNA transcript revealed that two ribozymes were able to cleave this substrate, showing a decrease in catalytic efficiency to 1/30 and 1/300 of the short substrate. This study indicates that the GUC triplet located at nucleotide 510 of the mRNA of IL-6 is the best site for hammerhead ribozyme-mediated cleavage. We suggest that in future targeting of chemically modified hammerhead ribosomes for cleavage of IL-6 RNA should be directed at this location. [less ▲]

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See detailCloning and Sequencing of the Dnak Locus in Streptomyces Coelicolor A3(2)
Brans, Alain ULg; Loriaux, Axelle; Joris, Bernard ULg et al

in DNA Sequence : The Journal of DNA Sequencing & Mapping (1996), 6(3), 179-84

The dnaK operon of Streptomyces coelicolor A3(2) was cloned by the DNA-probing method using synthetic oligonucleotides designed on the basis of two of the most conserved regions in 30 different DnaK ... [more ▼]

The dnaK operon of Streptomyces coelicolor A3(2) was cloned by the DNA-probing method using synthetic oligonucleotides designed on the basis of two of the most conserved regions in 30 different DnaK proteins (HSP70). The isolated insert-a BamHI 5.6-kb fragment-was sequenced and shown to contain three open-reading frames organized in an operon and coding for proteins analogous to DnaK, GrpE and DnaJ, successively. [less ▲]

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See detailCodon adjustment to maximise heterologous gene expression in Streptomyces lividans can lead to decreased mRNA stability and protein yield.
Lammertyn, E; Van Mellaert, L; Bijnens, A P et al

in Molecular & General Genetics [=MGG] (1996), 250(2), 223-9

The impact of the codon bias of the mouse tumour necrosis factor alpha (mTNF) gene cloned in Streptomyces lividans on the efficiency of expression and secretion was analysed. Minor codons occurring in the ... [more ▼]

The impact of the codon bias of the mouse tumour necrosis factor alpha (mTNF) gene cloned in Streptomyces lividans on the efficiency of expression and secretion was analysed. Minor codons occurring in the mTNF gene were therefore adapted to the codon bias of Streptomyces by site-directed mutagenesis. No improvement in mTNF yield could be detected. The stability of the transcript derived from the construct was shown to be more important for determining the final level of mTNF production. A strong correlation was observed between the yield of secreted biologically active mTNF and the amount of mTNF mRNA present in the cells. [less ▲]

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See detailAntipeptide antibody against the bovine IGF-BP-2 : application to the detection of BST-treated cows
Scippo, Marie-Louise ULg; Degand, Guy ULg; Duyckaerts, Anne et al

in Food & Agricultural Immunology (1996), 8

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See detailAmpd, Essential for Both Beta-Lactamase Regulation and Cell Wall Recycling, Is a Novel Cytosolic N-Acetylmuramyl-L-Alanine Amidase
Jacobs, Christine ULg; Joris, Bernard ULg; Jamin, M. et al

in Molecular Microbiology (1995), 15(3), 553-9

In enterobacteria, the ampD gene encodes a cytosolic protein which acts as a negative regulator of beta-lactamase expression. It is shown here that the AmpD protein is a novel N-acetylmuramyl-L-alanine ... [more ▼]

In enterobacteria, the ampD gene encodes a cytosolic protein which acts as a negative regulator of beta-lactamase expression. It is shown here that the AmpD protein is a novel N-acetylmuramyl-L-alanine amidase (E.C.3.5.1.28) participating in the intracellular recycling of peptidoglycan fragments. Surprisingly, AmpD exhibits an exclusive specificity for substrates containing anhydro muramic acid. This anhydro bond is mainly found in the peptidoglycan degradation products formed by the periplasmic lytic transglycosylases and thus might behave as a 'recycling tag' allowing the enzyme to distinguish these fragments from the newly synthesized peptidoglycan precursors. The AmpD substrate (or substrates) which accumulates in the absence of the corresponding enzymatic activity acts as an intracellular positive effector for beta-lactamase expression and might represent an element of a communication network between the chromosome and the cell wall peptidoglycan. [less ▲]

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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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