Open AccessControl of the activity of the soluble lytic transglycosylase by the stringent response in Escherichia coli
Author(s) -
Betzner A.S.,
Ferreira L.C.S.,
Höltje J.V.,
Keck W.
Publication year - 1990
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1990.tb13855.x
Subject(s) - lytic cycle , escherichia coli , microbiology and biotechnology , stringent response , enterobacteriaceae , biology , chemistry , virology , biochemistry , virus , gene
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 rel A + but not in rel A − cells. These findings indicate that the stringent control modulates the enzymatic activity of the soluble lytic transglycosylase in vivo.