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Control of the activity of the soluble lytic transglycosylase by the stringent response in Escherichia coli
28
Citations
13
References
1990
Year
Escherichia ColiEnzymatic ModificationSoluble Lytic TransglycosylaseProtein SynthesisBiosynthesisStructure-function Enzyme KineticsGlycosylationProtein GlycosylationBiochemistryMolecular MicrobiologyProtein BiosynthesisMetabolic PathwaysCellular EnzymologyNatural SciencesEnzyme CatalysisMicrobiologyRapid AutolysisCellular BiochemistryMedicineStringent Response
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.
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