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Structural and biochemical characterisation of the Providencia stuartii arginine decarboxylase shows distinct polymerisation and regulation

Bacterial homologous lysine and arginine decarboxylases play major roles in the acid stress response, physiology, antibiotic resistance and virulence. The Escherichia coli enzymes are considered as their archetypes. Whereas acid stress triggers polymerisation of the E. coli lysine decarboxylase LdcI...

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Autores principales: Jessop, Matthew, Huard, Karine, Desfosses, Ambroise, Tetreau, Guillaume, Carriel, Diego, Bacia-Verloop, Maria, Mas, Caroline, Mas, Philippe, Fraudeau, Angélique, Colletier, Jacques-Philippe, Gutsche, Irina
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8983666/
https://www.ncbi.nlm.nih.gov/pubmed/35383285
http://dx.doi.org/10.1038/s42003-022-03276-1
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author Jessop, Matthew
Huard, Karine
Desfosses, Ambroise
Tetreau, Guillaume
Carriel, Diego
Bacia-Verloop, Maria
Mas, Caroline
Mas, Philippe
Fraudeau, Angélique
Colletier, Jacques-Philippe
Gutsche, Irina
author_facet Jessop, Matthew
Huard, Karine
Desfosses, Ambroise
Tetreau, Guillaume
Carriel, Diego
Bacia-Verloop, Maria
Mas, Caroline
Mas, Philippe
Fraudeau, Angélique
Colletier, Jacques-Philippe
Gutsche, Irina
author_sort Jessop, Matthew
collection PubMed
description Bacterial homologous lysine and arginine decarboxylases play major roles in the acid stress response, physiology, antibiotic resistance and virulence. The Escherichia coli enzymes are considered as their archetypes. Whereas acid stress triggers polymerisation of the E. coli lysine decarboxylase LdcI, such behaviour has not been observed for the arginine decarboxylase Adc. Here we show that the Adc from a multidrug-resistant human pathogen Providencia stuartii massively polymerises into filaments whose cryo-EM structure reveals pronounced differences between Adc and LdcI assembly mechanisms. While the structural determinants of Adc polymerisation are conserved only in certain Providencia and Burkholderia species, acid stress-induced polymerisation of LdcI appears general for enterobacteria. Analysis of the expression, activity and oligomerisation of the P. stuartii Adc further highlights the distinct properties of this unusual protein and lays a platform for future investigation of the role of supramolecular assembly in the superfamily or arginine and lysine decarboxylases.
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spelling pubmed-89836662022-04-22 Structural and biochemical characterisation of the Providencia stuartii arginine decarboxylase shows distinct polymerisation and regulation Jessop, Matthew Huard, Karine Desfosses, Ambroise Tetreau, Guillaume Carriel, Diego Bacia-Verloop, Maria Mas, Caroline Mas, Philippe Fraudeau, Angélique Colletier, Jacques-Philippe Gutsche, Irina Commun Biol Article Bacterial homologous lysine and arginine decarboxylases play major roles in the acid stress response, physiology, antibiotic resistance and virulence. The Escherichia coli enzymes are considered as their archetypes. Whereas acid stress triggers polymerisation of the E. coli lysine decarboxylase LdcI, such behaviour has not been observed for the arginine decarboxylase Adc. Here we show that the Adc from a multidrug-resistant human pathogen Providencia stuartii massively polymerises into filaments whose cryo-EM structure reveals pronounced differences between Adc and LdcI assembly mechanisms. While the structural determinants of Adc polymerisation are conserved only in certain Providencia and Burkholderia species, acid stress-induced polymerisation of LdcI appears general for enterobacteria. Analysis of the expression, activity and oligomerisation of the P. stuartii Adc further highlights the distinct properties of this unusual protein and lays a platform for future investigation of the role of supramolecular assembly in the superfamily or arginine and lysine decarboxylases. Nature Publishing Group UK 2022-04-05 /pmc/articles/PMC8983666/ /pubmed/35383285 http://dx.doi.org/10.1038/s42003-022-03276-1 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Jessop, Matthew
Huard, Karine
Desfosses, Ambroise
Tetreau, Guillaume
Carriel, Diego
Bacia-Verloop, Maria
Mas, Caroline
Mas, Philippe
Fraudeau, Angélique
Colletier, Jacques-Philippe
Gutsche, Irina
Structural and biochemical characterisation of the Providencia stuartii arginine decarboxylase shows distinct polymerisation and regulation
title Structural and biochemical characterisation of the Providencia stuartii arginine decarboxylase shows distinct polymerisation and regulation
title_full Structural and biochemical characterisation of the Providencia stuartii arginine decarboxylase shows distinct polymerisation and regulation
title_fullStr Structural and biochemical characterisation of the Providencia stuartii arginine decarboxylase shows distinct polymerisation and regulation
title_full_unstemmed Structural and biochemical characterisation of the Providencia stuartii arginine decarboxylase shows distinct polymerisation and regulation
title_short Structural and biochemical characterisation of the Providencia stuartii arginine decarboxylase shows distinct polymerisation and regulation
title_sort structural and biochemical characterisation of the providencia stuartii arginine decarboxylase shows distinct polymerisation and regulation
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8983666/
https://www.ncbi.nlm.nih.gov/pubmed/35383285
http://dx.doi.org/10.1038/s42003-022-03276-1
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