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Volume 144, Issue 8

Membrane-bound and extracellular β-lactamase production with developmental regulation in Streptomyces griseus NRRL B-2682 Free

Abstract

A new type ofβ-lactamase has been isolated and characterized in NRRL B-2682. The enzyme has membrane-bound and extracellular forms. Biochemical characterization of some of the properties of the enzyme showed that it belongs to the class A group of penicillinases. Comparison of the membrane-bound and extracellular forms of theβ-lactamases suggests that they seem to be differently processed forms of the same enzyme. The N-terminal amino acid sequence of the extracellular form of the β-lactamase showed a high degree of similarity to a D-aminopeptidase of another strain. Secretion of the β-lactamase was affected by the differentiation state of the strain since in spontaneous non-sporulating mutants only the membrane-bound form was present. In accordance with this when sporulation of the wild-type strain was inhibited it failed to secrete extracellular β-lactamase. Addition of globomycin to the non-sporulating cells liberated the enzyme from the membrane, indicating that the protein is processed normally by signal peptidase II and a glyceride-thioether group, together with a fatty acid amide-linkage, is responsible for the attachment of the enzyme to the cellular membrane. Under sporulation-repressed conditions addition of peptidoglycan fragments and analogues or inhibition of cell wall biosynthesis by penicillin-G induced β-lactamase secretion and also restored sporulation both in solid and submerged cultures. These results confirm that β-lactamase secretion is tightly coupled to the sporulation process in .

  • Received:
  • Accepted:
  • Revised:
  • Published Online:
Keyword(s): sporulation , Streptomyces griseus and β-lactamase
© Society for General Microbiology 1998
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1998-08-01
2024-04-18
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Membrane-bound and extracellular β-lactamase production with developmental regulation in Streptomyces griseus NRRL B-2682
Microbiology 144, 2169 (1998); https://doi.org/10.1099/00221287-144-8-2169
/content/journal/micro/10.1099/00221287-144-8-2169
/content/journal/micro/10.1099/00221287-144-8-2169
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