1992
DOI: 10.1128/jb.174.9.2834-2842.1992
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Nucleotide sequence and transcriptional analysis of activator-regulator proteins for beta-lactamase in Streptomyces cacaoi

Abstract: The nucleotide sequence of the 2.7-kb DNA fragment upstream of the structural gene of beta-lactamase in Streptomyces cacaoi was determined. Computer-aided "FRAME" analysis revealed four possible open reading frames (ORFs), three in one direction and one in the opposite direction. One of them (ORF1, BlaA) encoded an activator-regulator protein whose deduced amino acid sequence was similar to that of other activator-regulator proteins in bacteria. Insertion of an 8-bp BamHI linker into the BlaA region decreased … Show more

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Cited by 18 publications
(19 citation statements)
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“…The deduced SmeR protein was compared with those of other ␤-lactamase regulators of the LysR family, namely, (i) AmpR proteins of the class C cephalosporinase systems of E. cloacae (14), C. freundii (16), Y. enterocolitica (32), and P. aeruginosa (18), (ii) AmpR for the class A ␤-lactamase from the gram-negative bacterium Rhodobacter capsulata (6), (iii) AmpR for the class A ␤-lactamase from the gram-positive actinomycetale Streptomyces cacaoi (36), (iv) the NmcR regulator of the class A carbapenem-hydrolyzing ␤-lactamase of E. cloacae NOR-1 (22), and (v) the type protein of the LysR family, LysR, for the lysine biosynthesis pathway of Escherichia coli (34). A dendrogram was derived to show the relatedness of these LysR family proteins by using the phylogeny package PAUP (Phylogenetic Analysis Using Parsimony), version 3.1 (35).…”
Section: Methodsmentioning
confidence: 99%
“…The deduced SmeR protein was compared with those of other ␤-lactamase regulators of the LysR family, namely, (i) AmpR proteins of the class C cephalosporinase systems of E. cloacae (14), C. freundii (16), Y. enterocolitica (32), and P. aeruginosa (18), (ii) AmpR for the class A ␤-lactamase from the gram-negative bacterium Rhodobacter capsulata (6), (iii) AmpR for the class A ␤-lactamase from the gram-positive actinomycetale Streptomyces cacaoi (36), (iv) the NmcR regulator of the class A carbapenem-hydrolyzing ␤-lactamase of E. cloacae NOR-1 (22), and (v) the type protein of the LysR family, LysR, for the lysine biosynthesis pathway of Escherichia coli (34). A dendrogram was derived to show the relatedness of these LysR family proteins by using the phylogeny package PAUP (Phylogenetic Analysis Using Parsimony), version 3.1 (35).…”
Section: Methodsmentioning
confidence: 99%
“…Furthermore, this system has been found to regulate virF, the master regulator of virulence genes in Shigella sonnei [53,54]. pSC-B78 demonstrated similarity to BlaA of Streptomyces cacaoi, which has been shown to regulate â-lactamase expression [55]. pSC-A46 was widely distributed among B. pseudomallei strains (Fig.…”
Section: Nucleotide Sequence Analysis Of Subtracted Librarymentioning
confidence: 99%
“…cloacae (Naas & Nordmann, 1994), the LysR-like proteins act as positive regulators both in the absence and in the presence of a b-lactam inducer. Such LysR-like proteins acting as positive regulators are also involved in the regulation of b-lactamases in Gram-positive bacteria such as Streptomyces cacaoi (Urabe & Ogawara, 1992). BlaP and BlaZ b-lactamase secretion is also induced in Bacillus licheniformis and Staphylococcus aureus, respectively, in the presence of exogenous inducers (Joris et al, 1994;Philippon et al, 1998).…”
Section: Introductionmentioning
confidence: 99%