Nucleotide sequence of the gene encoding the Streptomyces albus G beta-lactamase precursor

Dehottay, Philippe; Dusart, Jean; Meester, Fabien De; Joris, Bernard; Beeumen, Jozef Van; Erpicum, T.; Frère, Jean‐Marie; Ghuysen, Jean‐Marie

doi:10.1111/j.1432-1033.1987.tb13521.x

Cited by 67 publications

(37 citation statements)

References 24 publications

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“…After 20 min of incubation, the reaction mixture was lyophilized and spotted on 0.5-mm-thick silica gel thin-layer chromatography plates (DC-Fertigplatten 60; Merck, Darmstadt, Germany). The complete reaction mixture was lyophilized and suspended in 8 IlI of water, and 6 1.l was spotted on the plates. The plates were developed with isopropylic alcohol-water (85:15).…”

Section: Methodsmentioning

confidence: 99%

“…Several genes encoding extracellular enzymes have been cloned from Streptomyces species. These include endoglycosidase H (25), tyrosinase (16), agarase (4,17), P-lactamase (8), a-amylase (2,14,20,21,32,33), and xylanase (15,22). We have cloned in Streptomyces lividans the gene encoding a-amylase of Streptomyces griseus IMRU 3570 (31), a strain which is known to overproduce several extracellular enzymes (7).…”

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confidence: 99%

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Characterization, expression in Streptomyces lividans, and processing of the amylase of Streptomyces griseus IMRU 3570: two different amylases are derived from the same gene by an intracellular processing mechanism

et al. 1991

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Extracellular amylase in Streptomyces lividans was undetectable in starch-supplemented medium. However, S. lividans produced fivefold-higher levels of amylase than Streptomyces griseus IMRU 3570 when transformed with the S. griseus amy gene. Two major proteins of 57 and 50 kDa with amylase activity accumulated in the culture broths of the donor S. gniseus and S. lividans transformed with the amy gene. Both proteins were also present in protoplast lysates in the same relative proportion; they gave a positive reaction with antibodies against the 57-kDa amylase. They did not differ in substrate specificity or enzyme kinetics. The two amylases were purified to homogeneity by a two-step procedure. Both proteins showed the same amino-terminal sequence of amino acids, suggesting that both proteins are derived from the same gene. The deduced signal peptide has 28 amino acids with two positively charged arginines near the amino-terminal end. When an internal NcoI fragment was removed from the amy gene, the resulting S. lividans transformants did not synthesize any of the two amylase proteins and showed no reaction in immunoblotting. Formation of the 50-kDa protein was observed when pure 57-kDa amylase was treated with supernatants of protoplast lysates but not when it was treated with membrane preparations, indicating that the native 57-kDa amylase could be processed intracellularly.A large number of extracellular enzymes are produced by Streptomyces species that are used by these saprophytic microorganisms to degrade polymeric nutrients in soil originating from decaying plant material. Several genes encoding extracellular enzymes have been cloned from Streptomyces species. These include endoglycosidase H (25), tyrosinase (16), agarase (4, 17), P-lactamase (8), a-amylase (2,14,20,21,32,33), and xylanase (15,22). We have cloned in Streptomyces lividans the gene encoding a-amylase of Streptomyces griseus IMRU 3570 (31), a strain which is known to overproduce several extracellular enzymes (7). It contains an open reading frame of 1,698 nucleotides which encodes a protein with a deduced molecular mass of 59,713 Da.Very little is known, however, about the mechanisms of posttranslational modification and secretion of extracellular enzymes of Streptomyces species. Secretion of extracellular enzymes in Bacillus species and other bacteria proceeds by membrane anchoring of the amino-terminal end of the newly synthesized intracellular protein (24). The interaction of the amino-terminal hydrophobic region of the protein (the leader peptide) produces a modification of the protein phospholipid arrangement of the lipid bilayer that results in the opening of channels through which the protein is secreted. Passage of the extracellular protein through the secretion channels results in the cleavage of the leader peptide by the signal peptidase (23,24).In Streptomyces species, the leader peptides of extracellular proteins are poorly known, and no detailed studies on the protein-processing mechanisms prior to or during the secretion have bee...

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Section: Methodsmentioning

confidence: 99%

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confidence: 99%

Characterization, expression in Streptomyces lividans, and processing of the amylase of Streptomyces griseus IMRU 3570: two different amylases are derived from the same gene by an intracellular processing mechanism

et al. 1991

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“…(37,42), Streptomyces spp. (17,18), and Klebsiella spp. (3,4); plasmid-mediated enzymes from Staphylococcus aureus PC1 (46); and TEM-and SHV-type enzymes from members of the family Enterobacteriaceae (2,6,43).…”

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Sequence and molecular characterization of the ROB-1 beta-lactamase gene from Pasteurella haemolytica

Livrelli

Péduzzi

Joly

1991

Antimicrob Agents Chemother

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The ROB-1 ,I-lactamase-encoding plasmids from eight Pasteurella and two Haemophilus strains were compared by restriction endonuclease and hybridization analyses. Two types of ROB-i-encoding plasmids, which differed in size, were detected. One (4.1 kb) was found only in Pasteurella strains. The other (4.4 kb) was found in both Haemophilus influenzae and in one of the eight Pasteurella strains examined. These two plasmids shared multiple homologous fragments, suggesting that one was derived from the other. The ROB-i-encoding gene from Pasteurella P-Lactamases are the major determinants of resistance to P-lactam antibiotics among microorganisms and are widely distributed in both gram-positive and gram-negative bacteria (11). These enzymes were first classified according to their substrate profiles, isoelectric points, and other properties such as molecular weight. A classification scheme based on amino acid composition and sequence homologies was later proposed by Ambler (1), who defined classes A and B.3-Lactamases are now divided into four classes. Class A includes serine penicillinases such as chromosomally encoded 13-lactamases from Bacillus spp. (37, 42), Streptomyces spp. (17, 18), and Klebsiella spp. (3, 4); plasmid-mediated enzymes from Staphylococcus aureus PC1 (46); and TEM-and SHV-type enzymes from members of the family Enterobacteriaceae (2,6,43). All these class A P-lactamases show amino acid sequence homology, especially around the active serine site. Class B includes metalloenzymes (1), class C includes chromosomally encoded cephalosporinases (24), and class D includes oxacillinases (23). Most ,-lactamases have not yet been classified according to this scheme because their amino acid sequences are not available.The ROB-1 ,B-lactamase was first described in a human Haemophilus influenzae strain. The new enzyme had a TEM-like substrate profile, and its isoelectric point was estimated to be 8.1. In this strain ROB-1 was encoded by a plasmid of 4.4 kb, RROb (40). ROB-1 was later found in several H. influenzae strains and in porcine Actinobacillus pleuropneumoniae strains throughout the United States (34). More recently, in France we found (31) bovine and porcine Pasteurella multocida, Pasteurella haemolytica, and Pasteurella aerogenes strains that produce ROB-1. Furthermore, study of a ROB-1-encoding plasmid from an H. influenzae strain isolated in France revealed that it is identical to the 4.4-kb plasmid RROb (30).Recently, the nucleotide sequence of the ROB-1 13-lacta-* Corresponding author.mase gene from H. influenzae plasmid RROb was determined (26). We report here the molecular characterization of the ROB-1-encoding plasmids from Pasteurella and Haemophilus strains. The nucleotide sequence of the ,-lactamase gene from P. haemolytica LNPB 51 was determined, and the deduced amino acid sequence was compared with those of other enzymes. Our data confirmed that ROB-1 is a class A 13-lactamase which shares several features with gram-positive bacterial 1-lactamases. MATERIALS AND METHODSBacterial strain...

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“…The start codon was GUG, which had been previously defined to occur as start codon of ,B-lactamase genes from Streptomyces spp. (12,24) and tet(L) genes from Bacillus spp. (19,36,40,41).…”

Section: Discussionmentioning

confidence: 99%

Nucleotide sequence and phylogeny of the tet(L) tetracycline resistance determinant encoded by plasmid pSTE1 from Staphylococcus hyicus

Schwarz

Cardoso

Wegener

1992

Antimicrob Agents Chemother

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Nucleotide sequence of the gene encoding the Streptomyces albus G beta-lactamase precursor

Cited by 67 publications

References 24 publications

Characterization, expression in Streptomyces lividans, and processing of the amylase of Streptomyces griseus IMRU 3570: two different amylases are derived from the same gene by an intracellular processing mechanism

Characterization, expression in Streptomyces lividans, and processing of the amylase of Streptomyces griseus IMRU 3570: two different amylases are derived from the same gene by an intracellular processing mechanism

Sequence and molecular characterization of the ROB-1 beta-lactamase gene from Pasteurella haemolytica

Nucleotide sequence and phylogeny of the tet(L) tetracycline resistance determinant encoded by plasmid pSTE1 from Staphylococcus hyicus

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