Abstract
The ComX pheromone is an extracellular signaling molecule that stimulates natural competence in response to crowding in the Gram-positive bacterium Bacillus subtilis. The pheromone is formed by isoprenylation of an inactive precursor peptide, but its precise structure is not known. Here we report the structure of the ComX pheromone, showing that addition of a geranyl group to a tryptophan residue results in the formation of an unusual ring structure.
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Acknowledgements
The work performed in Nagoya was supported by Grants-in-Aid for Centers of Excellence (13CE2005 and 14COEA02) and for Scientific Research (No. 16580087). The work in Newark was supported by US National Institutes of Health grant GM57720.
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Supplementary information
Supplementary Fig. 1
1H NMR spectra of natural ComXRO-E-2 and synthetic ComXRO-E-2. (PDF 98 kb)
Supplementary Fig. 2
The DQF-COSY spectra of ComXRO-E-2. (PDF 121 kb)
Supplementary Fig. 3
The ROESY spectra of ComXRO-E-2. (PDF 84 kb)
Supplementary Fig. 4
Conformational analysis of a model of modified tryptophan 2. (PDF 52 kb)
Supplementary Table 1
1H NMR chemical shifts and coupling constants of geranyl groups and modified tryptophan residues in the natural ComXRO-E-2 pheromone and in synthetic peptides. (PDF 37 kb)
Supplementary Scheme 1
Purification scheme of the ComXRO-E-2 pheromone. (PDF 488 kb)
Supplementary Scheme 2
Synthetic scheme of ComXRO-E-2. (PDF 691 kb)
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Okada, M., Sato, I., Cho, S. et al. Structure of the Bacillus subtilis quorum-sensing peptide pheromone ComX. Nat Chem Biol 1, 23–24 (2005). https://doi.org/10.1038/nchembio709
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DOI: https://doi.org/10.1038/nchembio709
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