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Sublancin is not a lantibiotic but an S-linked glycopeptide

Nature Chemical Biology volume 7, pages 7880 (2011) | Download Citation

Abstract

Sublancin is shown to be an S-linked glycopeptide containing a glucose attached to a cysteine residue, establishing a new post-translational modification. The activity of the S-glycosyl transferase was reconstituted in vitro, and the enzyme is shown to have relaxed substrate specificity, allowing the preparation of analogs of sublancin. Glycosylation is essential for its antimicrobial activity.

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Acknowledgements

This work was supported by the US National Institutes of Health (GM58822 to W.A.v.d.D.) and a US National Institutes of Health Cellular and Molecular Biology Training Grant (T32 GM007283 to T.J.O.). X.N.O. was supported by the EXROP summer research program of the Howard Hughes Medical Institute.

Author information

Affiliations

  1. Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA.

    • Trent J Oman
    • , John M Boettcher
    • , Huan Wang
    •  & Wilfred A van der Donk
  2. Howard Hughes Medical Institute, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA.

    • Trent J Oman
    • , John M Boettcher
    • , Huan Wang
    •  & Wilfred A van der Donk
  3. College of Literature, Arts and Sciences, University of Michigan, Ann Arbor, Michigan, USA .

    • Xenia N Okalibe

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Contributions

T.J.O. performed mass spectrometric analyses and all biochemical assays shown, which were designed and analyzed by T.J.O. and W.A.v.d.D. J.M.B. performed NMR analysis. H.W. prepared and performed biochemical assays of the SunA mutant peptides. X.N.O. assisted with purification of sublancin and mass spectrometric analyses. T.J.O. and W.A.v.d.D. wrote the manuscript.

Competing interests

The authors declare no competing financial interests.

Corresponding author

Correspondence to Wilfred A van der Donk.

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DOI

https://doi.org/10.1038/nchembio.509

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