Control of the activity of the soluble lytic transglycosylase by the stringent response in Escherichia coli

• Published in: FEMS microbiology letters Vol. 55; no. 1-2; p. 161
• Main Authors: Betzner, A S, Ferreira, L C, Höltje, J V, Keck, W
• Format: Journal Article
• Language: English
• Published: England 15.01.1990
• Subjects: Amino Acids - pharmacology; Anti-Bacterial Agents - pharmacology; Autolysis; Escherichia coli - drug effects; Escherichia coli - enzymology; Glycosyltransferases; Guanosine Tetraphosphate - pharmacology; N-Acetylmuramoyl-L-alanine Amidase - antagonists & inhibitors; N-Acetylmuramoyl-L-alanine Amidase - metabolism; Protein Synthesis Inhibitors - pharmacology; Solubility; Transferases - antagonists & inhibitors; Transferases - metabolism
• ISSN: 0378-1097
• DOI: 10.1016/0378-1097(90)90187-U

The soluble lytic transglycosylase (Slt) of Escherichia coli is known to be a powerful murein hydrolase in vitro. It is shown here to act as an autolysin in vivo as well. Rapid autolysis of Slt overproducing cells was induced by protein biosynthesis inhibitors, which also block the fomration of guanosine-5'-diphosphate-3'-diphosphate (ppGpp). When amino acid starvation was used to inhibit protein synthesis, autolysis was suppressed in relA+ but not in relA- cells. These findings indicate that the stringent control modulates the enzymatic activity of the soluble lytic transglycosylase in vivo.