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The inhibition of elongation of Bacillus megaterium KM growing in the presence of low concentrations of nocardicin A resulted in the production of osmotically stable, actively dividing coccal-shaped cells. Saturation of penicillin-binding proteins 3a and 3b with nocardicin A in vivo at these concentrations was correlated with the inhibition of cell elongation. Analysis of the DD-carboxypeptidase activity of isolated vegetative membranes of B. megaterium KM in vitro indicated that penicillin-binding protein 4 is not a DD-carboxypeptidase under the assay conditions used. Penicillin-binding proteins were analysed by two-dimensional gel electrophoresis and the suitability of lysozyme treatment of cells as a method of membrane preparation was investigated with regard to the detection of proteins with highly labile penicillin-binding activities in vitro.

Type

Journal article

Journal

Eur J Biochem

Publication Date

15/11/1983

Volume

136

Pages

545 - 551

Keywords

Anti-Bacterial Agents, Bacillus megaterium, Bacterial Proteins, Binding, Competitive, Carrier Proteins, Chemical Phenomena, Chemistry, Electrophoresis, Polyacrylamide Gel, Hexosyltransferases, Lactams, Muramoylpentapeptide Carboxypeptidase, Penicillin-Binding Proteins, Peptidyl Transferases, Protein Binding