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Séminaire invité IBS

A new family of ribosomal peptide metallophores involved in bacterial adaptation to metal stress

​Vendredi 14 février 2025 à 11:00, Salle de séminaire IBS, 71 avenue des Martyrs, Grenoble

Publié le 14 février 2025
Françoise Jacob-Dubuisson
Centre d’infection et d’immunité de Lille​
Ribosomally synthesized, post-translationally modified peptides (RiPPs) form a large group of natural products employed by bacteria in their survival strategies. We recently discovered a new family of RiPPs that we called ‘bufferins’, as they are involved in copper homeostasis. Copper is a necessary but toxic transition metal, and hence bacteria have developed mechanisms that strictly control its homeostasis. We characterized the biosynthesis pathway of bufferins and showed that conserved cysteine residues are converted to rare post-translational modifications, thiooxazole groups, that are necessary for their metal-binding properties. With thousands of homologous biosynthetic gene clusters in the bacterial phylogenetic tree, bufferins represent a large family of metallophores and a widespread but overlooked metal homeostasis mechanism in bacteria.​

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