Chemical structure of posttranslational modification with A farnesyl group on tryptophan

Masahiro Okada, Hisao Yamaguchi, Isao Sato, Fumitada Tsuji, David Dubnau, Youji Sakagami

Research output: Contribution to journalArticle

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Bacillus subtilis and related bacilli produce a posttranslationally modified oligopeptide, the ComX pheromone, that stimulates natural genetic competence controlled by quorum sensing. The ComXRO-C-2 pheromone from strain RO-C-2 must be modified with a farnesyl group on the Trp residue, but the precise structure is not known. Here we report the precise nature of posttranslational farnesylation of ComXRO-C-2 pheromone on the Trp residue, resulting in the formation of a tricyclic structure. The ComX 168 pheromone, produced by the standard laboratory strain used in the study of B. subtilis, is also posttranslationally farnesylated according to phylogenetic resemblance.

Original languageEnglish (US)
Pages (from-to)914-918
Number of pages5
JournalBioscience, Biotechnology and Biochemistry
Issue number3
StatePublished - Apr 7 2008


All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry


  • Bacillus
  • ComX
  • Posttranslational modification
  • Quorum sensing
  • Tryptophan

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