PLoS ONE (Jan 2014)

A biochemical characterization of the DNA binding activity of the response regulator VicR from Streptococcus mutans.

  • Eduardo Ayala,
  • Jennifer S Downey,
  • Lauren Mashburn-Warren,
  • Dilani B Senadheera,
  • Dennis G Cvitkovitch,
  • Steven D Goodman

DOI
https://doi.org/10.1371/journal.pone.0108027
Journal volume & issue
Vol. 9, no. 9
p. e108027

Abstract

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Two-component systems (TCSs) are ubiquitous among bacteria and are among the most elegant and effective sensing systems in nature. They allow for efficient adaptive responses to rapidly changing environmental conditions. In this study, we investigated the biochemical characteristics of the Streptococcus mutans protein VicR, an essential response regulator that is part of the VicRK TCS. We dissected the DNA binding requirements of the recognition sequences for VicR in its phosphorylated and unphosphorylated forms. In doing so, we were able to make predictions for the expansion of the VicR regulon within S. mutans. With the ever increasing number of bacteria that are rapidly becoming resistant to even the antibiotics of last resort, TCSs such as the VicRK provide promising targets for a new class of antimicrobials.