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

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 gua...

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Bibliographic Details
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:
Autolysis
Bacteriology
Biological and medical sciences
Escherichia coli
Fundamental and applied biological sciences. Psychology
Metabolism. Enzymes
Microbiology
Murein
RelA
Salt
Soluble lytic transglycosylase
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Summary: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.
ISSN:0378-1097
1574-6968
DOI:10.1111/j.1574-6968.1990.tb13855.x