Gratuitous Synthesis of β-Lactamase in
            <i>Staphylococcus aureus</i>

Leggate, John; Holms, W. H.

doi:10.1128/jb.96.6.2110-2117.1968

Cited by 20 publications

(15 citation statements)

References 8 publications

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“…The appearance of a higher proportion of the faster form takes between 10 and 15 min in this assay. This correlates well with the appearance of measurable ␤-lactamase some 15 min after the addition of inducer in this system (data not shown), in agreement with the data of Leggate and Holms (1968). Furthermore, the DNAbinding experiments above demonstrate that intact Nand C-termini are absolutely required for the binding activity of the protein.…”

Section: Blai May Be Proteolytically Cleaved Upon Inductionsupporting

confidence: 88%

“…Substances capable of retarding the operator probe were sought in lysates of bacteria grown in the presence and absence of the ␤-lactamase inducer 2-(2Ј-carboxyphenyl)-benzoyl-6-aminopenicillanic acid (CBAP) at 5 g ml ¹1 (Leggate and Holms, 1968). Crude lysates were prepared from S. aureus RN4220 and RN4220(pOX416) without inducer and from RN4220(pOX416) with inducer.…”

Section: Induction Of the ␤-Lactamase System Eliminates The Binding Omentioning

confidence: 99%

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Studies of the repressor (BlaI) of β‐lactamase synthesis in Staphylococcus aureus

Gregory

Lewis

Curnock

et al. 1997

Molecular Microbiology

103

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SummaryPurified BlaI, the putative repressor of the ␤-lactamase operon in Staphylococcus aureus, binds specifically to two regions of dyad symmetry (operators) located in the blaZ-blaR1 intergenic region. BlaI binds with similar affinity to the two regions and to the related sequence upstream of the mec gene found in methicillin-resistant strains of S. aureus, providing physical evidence for the cross-talk previously observed between these systems. A change from a lysine in the N-terminus of BlaI to an alanine or deletion of the C-terminal 23 amino acids severely reduces its DNA-binding ability, demonstrating the functional importance of both the N-and C-termini. An operator DNA-protein complex observed with crude cell lysates from repressed cells, indistinguishable from that observed with purified BlaI, was eliminated by induction of the ␤-lactamase operon. Furthermore, BlaI is proteolytically cleaved in response to the addition of inducer in a blaR1-dependent manner, providing primary evidence for the molecular basis of induction. Thus, BlaI is shown to be the repressor of the ␤-lactamase system.

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Section: Blai May Be Proteolytically Cleaved Upon Inductionsupporting

confidence: 88%

Section: Induction Of the ␤-Lactamase System Eliminates The Binding Omentioning

confidence: 99%

Studies of the repressor (BlaI) of β‐lactamase synthesis in Staphylococcus aureus

Gregory

Lewis

Curnock

et al. 1997

Molecular Microbiology

103

View full text Add to dashboard Cite

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“…The culture was then divided into two flasks. A gratuitous inducer, 2(2'-carboxyphenyl)benzoyl-6-amino penicillanic acid (Imperial Chemical Industries, Ltd.), 7.5 Mg/ml, was added to one flask (16). Incubation with shaking was continued for 4 hr.…”

Section: Methodsmentioning

confidence: 99%

Phenotypic Suppression of Methicillin Resistance in Staphylococcus aureus by Mutant Noninducible Penicillinase Plasmids

1972

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Methicillin (intrinsic) resistance of Staphylococcus aureus was suppressed almost completely by regulatory gene (penIl) mutations of penicillinase plasmids that made penicillinase production strictly noninducible. Methicillin resistance was restored by secondary regulatory gene mutations that altered the noninducible phenotype or by complementation with a compatible plasmid that did not bear the noninducible mutation. No evidence was obtained for genetic linkage between a penicillinase plasmid and the gene for methicillin resistance. We suggest, therefore, that the mutant noninducible repressor acted in trans by binding to a site on the methicillin resistance determinant. This hypothesis would imply an appreciable degree of homology between penicillinase plasmids and methicillin resistance genes. 682 on July 16, 2020 by guest

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“…The production of at least some ,B-lactamase activity in all wild-type strains of B. cereus has been previously described (39). Even in S. aureus (which does not sporulate), ,B-lactamase induction has been shown to increase in the stationary phase of growth in response to 2, 2'-carboxyphenylbenzoyl-6-aminopenicilloic acid, a compound having minimal antibiotic activity (23).…”

Section: Position Ofmentioning

confidence: 98%

Derepression of β-Lactamase (Penicillinase) in Bacillus cereus by Peptidoglycans

1970

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In Bacillus cereus 569 a cellular inducer of,-lactamase was isolated which has the same constituents and basic structure as the soluble peptidoglycan found in sporulation, extracts from spores, and germination extracts, and which was previously called "spore-peptide." The material has been extensively purified and characterized. Two acid-soluble, high-molecular-weight peptidoglycan fractions containing muramic acid, glucosamine, diaminopimelic acid, D-aspartate, and D-and L-alanine, -lysine, -glycine, and -glutamate, distinguishable on the basis of size and different amino acid to amino sugar ratios, have been found to be responsible for the observed induction. Both fractions are capable of inducing high levels of 3-lactamase in concentrations lower than those of benzyl penicillin required for optimal induction. Several experiments also suggest that it is the accumulation of such soluble peptidoglycan in penicillin-treated cells which leads to induction of f3-lactamase and not the penicillin itself. The "spore-peptide" inducer becomes available during sporulation, and endogenous derepression ofj-lactamase activity occurs simultaneously. Such derepression also occurs in a strain of B. cereus very sensitive to penicillin and in which both uninduced as well as "spore-peptide"-induced #-lactamase is a small fraction of that produced by the typical penicillinase producer. These results suggest that ,B-lactamase in B. cereus functions in cell wall metabolism during sporulation. The hypothesis favored by many (see e.g., 34), that penicillinase evolved in bacteria as a result of offering selective advantage to producing cells by its ability to hydrolyze penicillin, has been questioned by others almost since the time the enzyme was isolated nearly 30 years ago. Indeed, Abraham, who fiast reported the presence of the I Portions of this work were used in partial fulfilment of the requirements for the Ph.thesda, Md. 20014. 52 the discovery of the transpeptidation reactions (43,46).Previous studies in this laboratory (36, 37) have shown that several cyclic and linear peptides as well as penicillins are capable of inducing high levels of ,B-lactamase in Staphylococcus aureus and Bacillus cereus 569. Since numerous peptides, both cyclic and linear, are produced by the genus Bacillus and since penicillin is also a cyclic peptide, we thought it feasible to look for inducing activity in cell-free preparations from B. cereus. Such an inducer has been isolated from sporulating cultures of B. cereus 569 and found to be a soluble peptidoglycan with inducing activity superior to that of penicillin. Other strains of B. cereus also produced indcing peptidoglycan. This report describes induction with the cellular inducer and presents its partial chemical characterization as well as evidence suggesting involvement of the a-type f3-lactamase of B. cereus in peptidoglycan metabolism during sporulation.

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Gratuitous Synthesis of β-Lactamase in Staphylococcus aureus

Cited by 20 publications

References 8 publications

Studies of the repressor (BlaI) of β‐lactamase synthesis in Staphylococcus aureus

Studies of the repressor (BlaI) of β‐lactamase synthesis in Staphylococcus aureus

Phenotypic Suppression of Methicillin Resistance in Staphylococcus aureus by Mutant Noninducible Penicillinase Plasmids

Derepression of β-Lactamase (Penicillinase) in Bacillus cereus by Peptidoglycans

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