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A novel subfamily of bacterial AAT-fold basic amino acid decarboxylases and functional characterization of its first representative: Pseudomonas aeruginosa LdcA

Diego Carriel 1 Pierre Simon Garcia 2 Florence Castelli 3 Patricia Lamourette 3 François Fenaille 3 Céline Brochier-Armanet 2 Sylvie Elsen 4 Irina Gutsche 1 
3 LEMM - Laboratoire d'Etude du Métabolisme des Médicaments
SPI - Service de Pharmacologie et Immunoanalyse : DRF/JOLIOT
4 PBRC - Pathogenèse bactérienne et réponses cellulaires
BCI - Biologie du Cancer et de l'Infection, CNRS - Centre National de la Recherche Scientifique : ERL 526
Abstract : Polyamines are small amino-acid derived polycations capable of binding negatively charged macromolecules. Bacterial polyamines are structurally and functionally diverse, and are mainly produced biosynthetically by pyridoxal-5-phosphate-dependent amino acid decarboxylases referred to as Lysine-Arginine-Ornithine decarboxylases (LAOdcs). In a phylogenetically limited group of bacteria, LAOdcs are also induced in response to acid stress. Here, we performed an exhaustive phylogenetic analysis of the AAT-fold LAOdcs which showcased the ancient nature of their short forms in Cyanobacteria and Firmicutes, and emergence of distinct subfamilies of long LAOdcs in Proteobacteria. We identified a novel subfamily of lysine decarboxylases, LdcA, ancestral in Betaproteobacteria and Pseudomonadaceae. We analyzed the expression of LdcA from Pseudomonas aeruginosa, and uncovered its role, intimately linked to cadaverine (Cad) production, in promoting growth and reducing persistence of this multidrug resistant human pathogen during carbenicillin treatment. Finally, we documented a certain redundancy in the function of the three main polyamines-Cad, putrescine (Put), and spermidine (Spd)-in P. aeruginosa by demonstrating the link between their intracellular level, as well as the capacity of Put and Spd to complement the growth phenotype of the ldcA mutant.
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Diego Carriel, Pierre Simon Garcia, Florence Castelli, Patricia Lamourette, François Fenaille, et al.. A novel subfamily of bacterial AAT-fold basic amino acid decarboxylases and functional characterization of its first representative: Pseudomonas aeruginosa LdcA. Genome Biology and Evolution, Society for Molecular Biology and Evolution, 2018, 10 (11), pp.3058-3075. ⟨10.1093/gbe/evy228⟩. ⟨hal-01987296⟩

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