Directed evolution of Vibrio fischeri LuxR signal sensitivity

Yuki Kimura, Yohei Tashiro, Kyoichi Saito, Shigeko Kawai-Noma, Daisuke Umeno*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)


LuxR is the core component of Vibrio fischeri quorum sensing. It acts as the transcriptional activator by binding to its cognate signaling molecules 3-oxo-hexanoyl-homoserine lactone (3OC6HSL). Although several acyl-HSLs with 3-oxo groups are known to activate LuxR with similar efficiency, acyl-HSLs without 3-oxo groups are very weak inducers. We conducted a round of LuxR directed evolution to acquire LuxR mutants with higher signal sensitivity to octanoyl-homoserine lactone (C8HSL). All of the isolated mutants showed increased signal sensitivity to many other acyl-HSLs, including C8HSL, and some to the LuxR antagonist p-coumaroyl-HSL. The evolution of their ligand sensitivity proceeded through the stabilization of the signal-bound state, thereby elevating the effective concentration of LuxR at the ON-state.

Original languageEnglish
Pages (from-to)533-538
Number of pages6
JournalJournal of Bioscience and Bioengineering
Issue number5
Publication statusPublished - 2016 Nov 1
Externally publishedYes


  • Antagonist
  • Chemical chaperone
  • Genetic switch
  • Positive selection
  • Quorum sensing
  • Synthetic biology

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology


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