Identification of a quorum sensing pheromone posttranslationally farnesylated at the internal tryptophan residue from Bacillus subtilis subsp. natto

Biosci Biotechnol Biochem. 2015;79(10):1567-9. doi: 10.1080/09168451.2015.1032884. Epub 2015 Apr 9.

Abstract

Bacillus subtilis subsp. natto produces poly-γ-glutamic acid under the control of quorum sensing. We identified ComXnatto pheromone as the quorum-sensing pheromone with an amino acid sequence of Lys-Trp-Pro-Pro-Ile-Glu and the tryptophan residue posttranslationally modified by a farnesyl group. ComXnatto pheromone is unique in the sense that the 5th tryptophan residue from the C-terminal is farnesylated.

Keywords: Bacillus subtilis; isoprenylation; posttranslational modification; quorum sensing; tryptophan.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacillus subtilis / genetics
  • Bacillus subtilis / metabolism*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Molecular Sequence Data
  • Pheromones / chemistry
  • Pheromones / genetics
  • Pheromones / metabolism*
  • Polyglutamic Acid / biosynthesis
  • Prenylation
  • Protein Processing, Post-Translational*
  • Protein Structure, Tertiary
  • Quorum Sensing / genetics*
  • Tryptophan / metabolism*

Substances

  • Bacterial Proteins
  • Pheromones
  • Polyglutamic Acid
  • Tryptophan