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Post-translational modification of ribosomally synthesized peptides by a radical SAM epimerase in Bacillus subtilis

Abstract : Ribosomally synthesized peptides are built out of L-amino acids, whereas D-amino acids are generally the hallmark of non-ribosomal synthetic processes. Here we show that the model bacterium Bacillus subtilis is able to produce a novel type of ribosomally synthesized and post-translationally modified peptide that contains D-amino acids, and which we propose to call epipeptides. We demonstrate that a two [4Fe-4S]-cluster radical S-adenosyl-L-methionine (SAM) enzyme converts L-amino acids into their D-counterparts by catalysing Cα-hydrogen-atom abstraction and using a critical cysteine residue as the hydrogen-atom donor. Unexpectedly, these D-amino acid residues proved to be essential for the activity of a peptide that induces the expression of LiaRS, a major component of the bacterial cell envelope stress-response system. Present in B. subtilis and in several members of the human microbiome, these epipeptides and radical SAM epimerases broaden the landscape of peptidyl structures accessible to living organisms.
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https://hal-normandie-univ.archives-ouvertes.fr/hal-01960697
Contributor : Jérôme Leprince <>
Submitted on : Wednesday, December 19, 2018 - 3:13:37 PM
Last modification on : Tuesday, September 8, 2020 - 5:34:01 PM

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Alhosna Benjdia, Alain Guillot, Pauline Ruffié, Jérôme Leprince, Olivier Berteau. Post-translational modification of ribosomally synthesized peptides by a radical SAM epimerase in Bacillus subtilis. Nature Chemistry, Nature Publishing Group, 2017, 9 (7), pp.698-707. ⟨10.1038/NCHEM.2714⟩. ⟨hal-01960697⟩

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