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

• Published in: FEMS microbiology letters 1990-01, Vol.67 (1-2), p.161-164
• Main Authors: Betzner, A.S., Ferreira, L.C.S., Höltje, J.-V., Keck, W.
• Format: Article
• Language: English
• Subjects: Amino Acids - pharmacology; Anti-Bacterial Agents - pharmacology; Autolysis; Escherichia coli - drug effects; Escherichia coli - enzymology; Glycosyltransferases; Guanosine Tetraphosphate - pharmacology; Murein; N-Acetylmuramoyl-L-alanine Amidase - antagonists & inhibitors; N-Acetylmuramoyl-L-alanine Amidase - metabolism; Protein Synthesis Inhibitors - pharmacology; RelA; Salt; Solubility; Soluble lytic transglycosylase; Transferases - antagonists & inhibitors; Transferases - metabolism
• ISSN: 0378-1097; 1574-6968
• 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 bio-synthesis inhibitors, which also block the fomration of guanosine-5′-diphosphate-3′-diphosphate (ppGpp). When amino acid starvation was used to 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.