Abstract
ComX, an oligopeptide pheromone that stimulates the natural genetic competence controlled by quorum sensing in Bacillus subtilis and related bacilli, contains a prenyl-modified tryptophan residue. Since ComX is the only protein known to contain prenylated tryptophan, the universality of this unique posttranslational modification has yet to be determined. Recently, we developed a cell-free assay system in which the tryptophan residue in the ComX RO-E-2 pheromone precursor derived from B. subtilis strain RO-E-2 can be geranylated by the ComQRO-E-2 enzyme. We report here our attempt to identify the consensus sequence surrounding the geranylated tryptophan residue by using the cellfree system with various ComXRO-E-2 pheromone precursor analogs. We found that [47-58]ComXRO-E-2, corresponding to the C-terminal 12-residue peptide of the pheromone precursor, contained a short sequence essential for geranylation. We also found that the length of the sequence between the tryptophan residue and the C-terminus was important for geranylation, and that some [47-58]ComXRO-E-2 pheromone precursor amino acids were involved in the geranylation reaction. However, we could not identify a consensus sequence surrounding the geranylated tryptophan. Our evidence suggests that, like Rab which lacks a consensus sequence yet is geranylgeranyl-modified on a cysteine residue, the ComX pheromone and its precursor also lack a consensus sequence.
Original language | English |
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Pages (from-to) | 1492-1496 |
Number of pages | 5 |
Journal | Bioscience, Biotechnology and Biochemistry |
Volume | 76 |
Issue number | 8 |
DOIs | |
Publication status | Published - 2012 |
Externally published | Yes |
Keywords
- Bacillus subtilis
- ComX pheromone
- Post-translational modification
- Prenylation
- Prenyltransferase
ASJC Scopus subject areas
- Biotechnology
- Analytical Chemistry
- Biochemistry
- Applied Microbiology and Biotechnology
- Molecular Biology
- Organic Chemistry