PMID:12949085
| Citation |
Meisel, U, Höltje, JV and Vollmer, W (2003) Overproduction of inactive variants of the murein synthase PBP1B causes lysis in Escherichia coli. J. Bacteriol. 185:5342-8 |
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| Abstract |
Penicillin-binding protein 1B (PBP1B) of Escherichia coli is a bifunctional murein synthase containing both a transpeptidase domain and a transglycosylase domain. The protein is present in three forms (alpha, beta, and gamma) which differ in the length of their N-terminal cytoplasmic region. Expression plasmids allowing the production of native PBP1B or of PBP1B variants with an inactive transpeptidase or transglycosylase domain or both were constructed. The inactive domains contained a single amino acid exchange in an essential active-site residue. Overproduction of the inactive PBP1B variants, but not of the active proteins, caused lysis of wild-type cells. The cells became tolerant to lysis by inactive PBP1B at a pH of 5.0, which is similar to the known tolerance for penicillin-induced lysis under acid pH conditions. Lysis was also reduced in mutant strains lacking several murein hydrolases. In particular, a strain devoid of activity of all known lytic transglycosylases was virtually tolerant, indicating that mainly the lytic transglycosylases are responsible for the observed lysis effect. A possible structural interaction between PBP1B and murein hydrolases in vivo by the formation of a multienzyme complex is discussed. |
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| Keywords |
Bacterial Proteins; Bacteriolysis/physiology; Carrier Proteins; Catalytic Domain; Cell Division/physiology; Enzyme Activation; Escherichia coli/physiology; Escherichia coli Proteins; Hexosyltransferases/genetics; Hexosyltransferases/metabolism; Hydrogen-Ion Concentration; Multienzyme Complexes/genetics; Multienzyme Complexes/metabolism; Muramoylpentapeptide Carboxypeptidase; Mutation; N-Acetylmuramoyl-L-alanine Amidase/genetics; N-Acetylmuramoyl-L-alanine Amidase/metabolism; Penicillin-Binding Proteins; Peptide Synthases/genetics; Peptide Synthases/metabolism; Peptidoglycan Glycosyltransferase; Peptidyl Transferases/genetics; Peptidyl Transferases/metabolism; Serine-Type D-Ala-D-Ala Carboxypeptidase |
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