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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Veröffentlicht in:FEMS microbiology letters 1990-01, Vol.67 (1-2), p.161-164
Hauptverfasser: Betzner, A.S., Ferreira, L.C.S., Höltje, J.-V., Keck, W.
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Sprache:eng
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Zusammenfassung: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:10.1016/0378-1097(90)90187-U