Exopenicillinase Synthesis in
            <i>Staphylococcus aureus</i>

Coles, N. W.; Gross, R

doi:10.1128/jb.98.2.659-661.1969

Cited by 5 publications

(2 citation statements)

References 7 publications

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“…Penicillinase is produced in Bacillus licheniformis by growing cells, although secretion of the o2 enzyme will continue even when growth is inhibited by chloramphenicol (2, 11). The exopeni-E cillinase of Staphylococcus aureus is secreted E only by cells in which de novo protein synthesis°i s occurring (3). Even a constitutive autolytic enzyme in Streptococcus faecalis is formed only when the cells are dividing (10,12).…”

Section: Discussionmentioning

confidence: 99%

Recovery of Exocellular Acid Phosphatase Activity on Saccharomyces mellis After Treatment of the Organism with Reagents That Affect the Cell Surface

Weimberg

1971

J Bacteriol

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Derepressed cells of Saccharomyces mellis were treated in one of several different ways to either elute or inactivate the exocellular enzyme, acid phosphatase. The enzyme was either (i) eluted from resting cells with 0.5 m KCl plus 0.1% β-mercaptoethanol, (ii) eluted from exponential phase cells by growing the organism in derepressing media containing 0.5 m KCl, or (iii) inactivated on exponential phase cells by adding sufficient acid or base to growth media to destroy the enzyme but not enough to kill the cells. These treatments did not affect viability. Treated cells were transferred to fresh growth media or some other reaction mixture, and the kinetics of recovery of acid phosphatase activity was studied. In these reaction mixtures, enzyme was synthesized only by actively growing cells. Treated resting cells were indistinguishable from untreated, repressed resting cells in that the organism inoculated into complete growth medium remained in the lag phase for approximately 6 hr before both growth and enzyme synthesis began. Exponential phase derepressed cells treated by method (ii) or (iii) were transferred to fresh medium under conditions that allowed growth to continue. The cells immediately started to manufacture enzyme at a rate greater than normal until the steady-state level was reached, thus demonstrating a feedback control system. Exponential phase repressed cells were also transferred to fresh derepressing media under conditions which sustained growth. Though these cells began to grow immediately, there was a lag before acid phosphatase synthesis began followed by a lengthy inductive period. The length of the period of induction could be correlated with the polyphosphate content of the cells. As the supply of polyphosphate neared exhaustion, the rate of synthesis increased rapidly until it was greater than normal; this differential rate was sustained until the steady-state concentration was reached. When derepressed cells grow in a medium containing 0.5 m KCl, some acid phosphatase activity is found free in the culture fluid and some remains firmly attached to the cells despite the presence of the salt. The bound activity is subject to feedback control, but the steady-state level of this activity on the cells is only one-third that of the acid phosphatase on cells growing in nonsaline media. The extracellular phosphatase is produced at a rate that is several-fold greater than that of the exocellular enzyme in a nonsaline medium. The synthesis of the extracellular enzyme does not seem to be controlled by a feedback mechanism but is produced at a maximal rate as long as the cells are growing.

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Section: Discussionmentioning

confidence: 99%

Recovery of Exocellular Acid Phosphatase Activity on Saccharomyces mellis After Treatment of the Organism with Reagents That Affect the Cell Surface

Weimberg

1971

J Bacteriol

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“…MATERIALS AND METHODS Bacterial strains. Two strains of' S. aureus inducible for penicillinase were used and have been described previously (3,4,6) together with their method of cultivation (6). The phage type 80/81 organism originally described has now been designated 2237.…”

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confidence: 99%

Preparation of Metabolically Active Staphylococcus aureus Protoplasts by Use of the Aeromonas hydrophila Lytic Enzyme

Coles

Gross

1973

J Bacteriol

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Stable, metabolically active protoplasts of Staphylococcus aureus have been prepared by the use of a staphylolytic enzyme produced by Aeromonas hydrophila. Respiratory and glycolytic rates and synthesis of nucleic acids, protein, and lipid in these protoplasts, stabilized variously in 1.1 M sucrose, 0.37 M sodium succinate, or 0.37 M sodium sulfate, have been shown to be comparable with the same parameters in intact cells under the same conditions.

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A Mechanism for Penicillinase Secretion in Bacillus licheniformis

Sargent

Lampen

1970

Proc. Natl. Acad. Sci. U.S.A.

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Abstract. Cell-bound isozymes of penicillinase are distinguished from extracellular enzyme by their capacity to bind deoxycholate and to elute with an apparent molecular weight of 45,000 on gel filtration in its presence. By methods that are unlikely to involve changes in primary structure, the cellbound forms (both from the plasma membrane and from the periplasmic vesicles) can be converted to forms that are very similar if not identical to the exo-form (i.e., eluting with a molecular weight of 24,000 in the presence and absence of deoxycholate). In the case of plasma membrane penicillinase, addition of 25 per cent potassium phosphate at pH 9.0 leads to a 65 per cent conversion in 20 minutes at 300. Vesicle fraction penicillinase can be converted by pH 9.0 treatment alone. We suggest that the conversion involves a change from a hydrophobic to a hydrophilic conformational type, and that this is the crucial step for enzyme secretion in microorganisms. A model is presented to account for existing data in which we postulate that monomers of the newly synthesized penicillinase in an extended hydrophobic conformation are inserted into the membrane at special growing points where they may change to a hydrophilic exoform, or polymerize to the major plasma membrane type of penicillinase.Introduction. For the study of enzyme secretion, a system is desirable in which there is a rate-limiting step between synthesis and release. Pollock was able to demonstrate that a part of the penicillinase synthesized by Bacillus licheniformis (strain 749) passed through a cell-bound state before release.1 Later, we showed that only about 25 per cent of the penicillinase secreted at any one time during active synthesis was derived from a cell-bound intermediate and the remainder was released by a process coupled to synthesis.2 Two entirely separate and different processes could be involved but it is equally possible to visualize a unified scheme of secretion which is only partly inhibited by chloramphenicol (see below).The cell-bound penicillinase is present in the plasma membrane and in a periplasmic vesicle fraction released by protoplasting.3 Chloramphenicol-insensi-

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Exopenicillinase Synthesis in Staphylococcus aureus

Cited by 5 publications

References 7 publications

Recovery of Exocellular Acid Phosphatase Activity on Saccharomyces mellis After Treatment of the Organism with Reagents That Affect the Cell Surface

Recovery of Exocellular Acid Phosphatase Activity on Saccharomyces mellis After Treatment of the Organism with Reagents That Affect the Cell Surface

Preparation of Metabolically Active Staphylococcus aureus Protoplasts by Use of the Aeromonas hydrophila Lytic Enzyme

A Mechanism for Penicillinase Secretion in Bacillus licheniformis

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