Leprevosta, Laura; Jüngerb, Sophie; Lippensc, Guy; Guillaumeb, Céline; Sicolid, Giuseppe; Oliveirae, Lydie; de Santis, Emiliano; Falconef, Enrico; Rivera-Millot, Alex; Billon, Gabriel; Stellato, Francesco; Henry, Céline; Antoine, Rudy; Zirah, Séverine; Dubiley, Svetlana; Li, Yanyan et Jacob-Dubuisson, Françoise (2024). A widespread family of ribosomal peptide metallophores involved in bacterial adaptation to metal stress Proceedings of the National Academy of Sciences of the United States of America , vol. 121 , nº 49. pp. 1-10. DOI: 10.1073/pnas.2408304121.
Ce document n'est pas hébergé sur EspaceINRS.Résumé
Ribosomally synthesized and posttranslationally modified peptides (RiPPs) are a structurally diverse group of natural products that bacteria employ in their survival strategies. Herein, we characterized the structure, the biosynthetic pathway, and the mode of action of a RiPP family called bufferins. With thousands of homologous biosynthetic gene clusters throughout the bacterial phylogenetic tree, bufferins form by far the largest family of RiPPs modified by multinuclear nonheme iron- dependent modification is installed in conjunction with a partner protein of the DUF2063 family. reveal that bufferins are involved in copper homeostasis, and their metal- binding under copper stress by complexing excess metal ions. Our study thus describes a homeostasis mechanism in bacteria.
| Type de document: | Article |
|---|---|
| Mots-clés libres: | Metallophore; Multinuclear non-heme iron-dependent oxidase (MNIO); Ribosomally synthesized and post-translationally modified peptide (RiPP) |
| Centre: | Centre INRS-Institut Armand Frappier |
| Date de dépôt: | 24 déc. 2024 22:34 |
| Dernière modification: | 24 déc. 2024 22:34 |
| URI: | https://espace.inrs.ca/id/eprint/16240 |
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