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Journal Article

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

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Betzner,  AS
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Ferreira,  LCS
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Höltje,  J-V
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Keck,  W
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Citation

Betzner, A., Ferreira, L., Höltje, J.-V., & Keck, W. (1990). Control of the activity of the soluble lytic transglycosylase by the stringent response in Escherichia coli. FEMS Microbiology Letters, 55(1-2), 161-164. doi:10.1016/0378-1097(90)90187-u.


Cite as: https://hdl.handle.net/21.11116/0000-000D-EA95-3
Abstract
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.