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

A new type of beta-lactamase has been isolated and characterized in Streptomyces griseus 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...

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Bibliographic Details
Published in:	Microbiology (Society for General Microbiology) Vol. 144; no. 8; pp. 2169 - 2177
Main Authors:	DEAK, E, SZABO, I, KALMACZHELYI, A, GAL, Z, BARABAS, G, PENYIGE, A
Format:	Journal Article
Language:	English
Published:	Reading Society for General Microbiology 01-08-1998
Subjects:	Acetylmuramyl-Alanyl-Isoglutamine - pharmacology Amino Acid Sequence Anti-Bacterial Agents - pharmacology Bacteriology beta-Lactamases - biosynthesis beta-Lactamases - isolation & purification Biological and medical sciences Extracellular Space - enzymology Extracellular Space - microbiology Fundamental and applied biological sciences. Psychology Membrane Proteins - metabolism Metabolism. Enzymes Microbiology Molecular Sequence Data Mutation N-Acetylmuramoyl-L-alanine Amidase - metabolism Penicillin G - pharmacology Peptide Fragments - pharmacology Peptides Peptidoglycan - pharmacology Protease Inhibitors - pharmacology Spores, Bacterial - drug effects Spores, Bacterial - enzymology Streptomyces griseus Streptomyces griseus - drug effects Streptomyces griseus - enzymology Streptomyces griseus - physiology Streptomycetaceae Enzyme Biosynthesis β-Lactamase Extracellular Actinomycetales Characterization Membrane enzyme Regulation(control) Sporulation Bacteria Hydrolases Actinomycetes Streptomyces griseus
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Summary:	A new type of beta-lactamase has been isolated and characterized in Streptomyces griseus 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 the beta-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 beta-lactamase showed a high degree of similarity to a D-aminopeptidase of another Streptomyces griseus strain. Secretion of the beta-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 beta-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 beta-lactamase secretion and also restored sporulation both in solid and submerged cultures. These results confirm that beta-lactamase secretion is tightly coupled to the sporulation process in S. griseus.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1350-0872 1465-2080
DOI:	10.1099/00221287-144-8-2169