Abstract
The Staphylococcus aureus autoinducer-2 (AI-2) producer protein LuxS is phosphorylated by the Ser/Thr kinase Stk1 at a unique position, Thr14. The enzymatic activity of the phosphorylated isoform of LuxS was abrogated compared to that of nonphosphorylated LuxS, thus providing the first evidence of an AI-2-producing enzyme regulated by phosphorylation and demonstrating that S. aureus possesses an original and specific system for controlling AI-2 synthesis.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism*
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Carbon-Sulfur Lyases / genetics
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Carbon-Sulfur Lyases / metabolism*
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Gene Expression Regulation, Bacterial*
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Homoserine / analogs & derivatives*
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Homoserine / biosynthesis
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Lactones
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Models, Biological
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Models, Molecular
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Molecular Sequence Data
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Phosphorylation
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Protein Serine-Threonine Kinases / metabolism*
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Protein Structure, Tertiary
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Sequence Alignment
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Staphylococcus aureus / genetics
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Staphylococcus aureus / metabolism
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Staphylococcus aureus / physiology*
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Threonine / metabolism
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Virulence Factors / metabolism*
Substances
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Bacterial Proteins
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Lactones
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N-octanoylhomoserine lactone
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Virulence Factors
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Threonine
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Homoserine
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Protein Serine-Threonine Kinases
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Stk1 protein, Staphylococcus aureus
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Carbon-Sulfur Lyases
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LuxS protein, Bacteria