The Staphylococcus aureus autoinducer-2 synthase LuxS is regulated by Ser/Thr phosphorylation

J Bacteriol. 2010 Dec;192(23):6295-301. doi: 10.1128/JB.00853-10. Epub 2010 Sep 24.

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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Carbon-Sulfur Lyases / genetics
  • Carbon-Sulfur Lyases / metabolism*
  • Gene Expression Regulation, Bacterial*
  • Homoserine / analogs & derivatives*
  • Homoserine / biosynthesis
  • Lactones
  • Models, Biological
  • Models, Molecular
  • Molecular Sequence Data
  • Phosphorylation
  • Protein Serine-Threonine Kinases / metabolism*
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Staphylococcus aureus / genetics
  • Staphylococcus aureus / metabolism
  • Staphylococcus aureus / physiology*
  • Threonine / metabolism
  • Virulence Factors / metabolism*

Substances

  • Bacterial Proteins
  • Lactones
  • N-octanoylhomoserine lactone
  • Virulence Factors
  • Threonine
  • Homoserine
  • Protein Serine-Threonine Kinases
  • Stk1 protein, Staphylococcus aureus
  • Carbon-Sulfur Lyases
  • LuxS protein, Bacteria