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Structure of the Bacillus subtilis quorum-sensing peptide pheromone ComX

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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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Figure 1: Amino acid sequence of the ComXRO-E-2 pheromone and structures of the modified tryptophan residue in the ComXRO-E-2 pheromone.
Figure 2: Dose-response curves obtained using the natural ComXRO-E-2 pheromone and the synthetic peptide 1a.

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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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Authors and Affiliations

  1. Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa-ku, Nagoya, 464-8601, Japan

    Masahiro Okada, Isao Sato, Hidehisa Iwata, Toshihiko Nishio & Youji Sakagami

  2. Public Health Research Institute, 225 Warren Street, Newark, 07103, New Jersey, USA

    Soo Jeong Cho & David Dubnau

Authors
  1. Masahiro Okada
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  2. Isao Sato
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  3. Soo Jeong Cho
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  4. Hidehisa Iwata
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  5. Toshihiko Nishio
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  6. David Dubnau
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  7. Youji Sakagami
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Corresponding authors

Correspondence to David Dubnau or Youji Sakagami.

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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)

Supplementary Methods (PDF 584 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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