Membrane-bound and extracellular beta-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 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.
Institute of Biology,University Medical School of DebrecenDebrecen, Nagyerdei krt. 98, H-4012 Hungary.
Eleonóra
E
Deák
Institute of Biology,University Medical School of DebrecenDebrecen, Nagyerdei krt. 98, H-4012 Hungary.
István
I
SzabóA
Institute of Biology,University Medical School of DebrecenDebrecen, Nagyerdei krt. 98, H-4012 Hungary.
Attila
A
Kálmáczhelyi
Institute of Pharmacology,University Medical School of DebrecenDebrecen, Nagyerdei krt. 98, H-4012 Hungary.
Zsuzsanna
Z
Gál
Institute of Biology,University Medical School of DebrecenDebrecen, Nagyerdei krt. 98, H-4012 Hungary.
György
G
Barabás
Institute of Biology Research Group for Microbial Developmental GeneticsMTA DOTE, Institute of Biology.|Institute of Biology,University Medical School of DebrecenDebrecen, Nagyerdei krt. 98, H-4012 Hungary.
Andres
A
Penyige
D000119:Acetylmuramyl-Alanyl-Isoglutamine / Q000494:pharmacology; D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000494:pharmacology; D005110:Extracellular Space / Q000201:enzymology* / Q000382:microbiology; D008565:Membrane Proteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D009154:Mutation; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000378:metabolism; D010400:Penicillin G / Q000494:pharmacology; D010446:Peptide Fragments / Q000494:pharmacology; D010455:Peptides; D010457:Peptidoglycan / Q000494:pharmacology; D011480:Protease Inhibitors / Q000494:pharmacology; D013171:Spores, Bacterial / Q000187:drug effects / Q000201:enzymology; D013305:Streptomyces griseus / Q000187:drug effects / Q000201:enzymology* / Q000502:physiology; D001618:beta-Lactamases / Q000096:biosynthesis* / Q000302:isolation & purification
D000900:Anti-Bacterial Agents; D008565:Membrane Proteins; D010446:Peptide Fragments; D010455:Peptides; D010457:Peptidoglycan; D011480:Protease Inhibitors; D000119:Acetylmuramyl-Alanyl-Isoglutamine; C017339:globomycin; D009238:N-Acetylmuramoyl-L-alanine Amidase; D001618:beta-Lactamases; D010400:Penicillin G