Academic Journal

Characterization of an acetyltransferase that detoxifies aromatic chemicals in Legionella pneumophila.

التفاصيل البيبلوغرافية
العنوان: Characterization of an acetyltransferase that detoxifies aromatic chemicals in Legionella pneumophila.
المؤلفون: Kubiak, Xavier, Dervins-Ravault, Delphine, Pluvinage, Benjamin, Chaffotte, Alain F, Gomez-Valero, Laura, Dairou, Julien, Busi, Florent, Dupret, Jean-Marie, Buchrieser, Carmen, Rodrigues-Lima, Fernando
المساهمون: Unité de Biologie Fonctionnelle et Adaptative (BFA (UMR_8251 / U1133)), Université Paris Diderot - Paris 7 (UPD7)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Biologie des Bactéries intracellulaires - Biology of Intracellular Bacteria, Institut Pasteur Paris (IP)-Centre National de la Recherche Scientifique (CNRS), Résonance Magnétique Nucléaire des Biomolécules, This work was supported by the Université Paris Diderot Paris 7, DGA (Délégation Générale de l’Armement), CAMPLP (Caisse d’Assurance Maladies des Professions Libérales de Province), the Institut Pasteur, the CNRS (Centre National de la Recherche) and the Institut Carnot-Pasteur MI., X.K. is supported by a fellowship from the Université Paris Diderot-Paris 7. B.P. was supported by a fellowship from the DGA. L.G.V. was holder of a Roux post-doctoral research fellowship financed by the Institut Pasteur and subsequently with support from the FRM (Fondation pour la Recherche Médicale). C.B. was funded by Pasteur MI and the French Region Ile de France (DIM Malinf).
المصدر: ISSN: 0264-6021.
بيانات النشر: HAL CCSD
Portland Press
سنة النشر: 2012
مصطلحات موضوعية: kinetics, enzyme variant, detoxification, arylamine N-acetyltransferase, Acetylation, MESH: Amines/metabolism, MESH: Arylamine N-Acetyltransferase/genetics, MESH: Arylamine N-Acetyltransferase/metabolism, MESH: Blotting, Western, MESH: Circular Dichroism, MESH: Genetic Complementation Test, MESH: Genetic Variation, MESH: Hydrocarbons, Aromatic/metabolism, MESH: Inactivation, Metabolic, MESH: Legionella pneumophila/classification, MESH: Legionella pneumophila/enzymology, MESH: Legionella pneumophila/genetics, MESH: Legionnaires' Disease/genetics, MESH: Legionnaires' Disease/microbiology, MESH: Phylogeny, MESH: Protein Folding, MESH: Recombinant Proteins/genetics, MESH: Recombinant Proteins/metabolism, [SDV.BC]Life Sciences [q-bio]/Cellular Biology
الوصف: International audience ; Legionella pneumophila is an opportunistic pathogen and the causative agent of Legionnaires' disease. Despite being exposed to many chemical compounds in its natural and man-made habitats (natural aquatic biotopes and man-made water systems), L. pneumophila is able to adapt and survive in these environments. The molecular mechanisms by which this bacterium detoxifies these chemicals remain poorly understood. In particular, the expression and functions of XMEs (xenobiotic-metabolizing enzymes) that could contribute to chemical detoxification in L. pneumophila have been poorly documented at the molecular and functional levels. In the present paper we report the identification and biochemical and functional characterization of a unique acetyltransferase that metabolizes aromatic amine chemicals in three characterized clinical strains of L. pneumophila (Paris, Lens and Philadelphia). Strain-specific sequence variations in this enzyme, an atypical member of the arylamine N-acetyltransferase family (EC 2.3.1.5), produce enzymatic variants with different structural and catalytic properties. Functional inactivation and complementation experiments showed that this acetyltransferase allows L. pneumophila to detoxify aromatic amine chemicals and grow in their presence. The present study provides a new enzymatic mechanism by which the opportunistic pathogen L. pneumophila biotransforms and detoxifies toxic aromatic chemicals. These data also emphasize the role of XMEs in the environmental adaptation of certain prokaryotes.
نوع الوثيقة: article in journal/newspaper
اللغة: English
Relation: info:eu-repo/semantics/altIdentifier/pmid/22545684; pasteur-01339052; https://pasteur.hal.science/pasteur-01339052; PUBMED: 22545684
DOI: 10.1042/BJ20120528
الاتاحة: https://pasteur.hal.science/pasteur-01339052
https://doi.org/10.1042/BJ20120528
رقم الانضمام: edsbas.70C4AA12
قاعدة البيانات: BASE