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A polyamine acetyltransferase regulates the motility and biofilm formation of Acinetobacter baumannii
Acinetobacter baumannii is a nosocomial pathogen highly resistant to environmental changes and antimicrobial treatments. Regulation of cellular motility and biofilm formation is important for its virulence, although it is poorly described at the molecular level. It has been previously reported that...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Nature Publishing Group UK
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10267138/ https://www.ncbi.nlm.nih.gov/pubmed/37316480 http://dx.doi.org/10.1038/s41467-023-39316-5 |
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author | Armalytė, Julija Čepauskas, Albinas Šakalytė, Gabija Martinkus, Julius Skerniškytė, Jūratė Martens, Chloé Sužiedėlienė, Edita Garcia-Pino, Abel Jurėnas, Dukas |
author_facet | Armalytė, Julija Čepauskas, Albinas Šakalytė, Gabija Martinkus, Julius Skerniškytė, Jūratė Martens, Chloé Sužiedėlienė, Edita Garcia-Pino, Abel Jurėnas, Dukas |
author_sort | Armalytė, Julija |
collection | PubMed |
description | Acinetobacter baumannii is a nosocomial pathogen highly resistant to environmental changes and antimicrobial treatments. Regulation of cellular motility and biofilm formation is important for its virulence, although it is poorly described at the molecular level. It has been previously reported that Acinetobacter genus specifically produces a small positively charged metabolite, polyamine 1,3-diaminopropane, that has been associated with cell motility and virulence. Here we show that A. baumannii encodes novel acetyltransferase, Dpa, that acetylates 1,3-diaminopropane, directly affecting the bacterium motility. Expression of dpa increases in bacteria that form pellicle and adhere to eukaryotic cells as compared to planktonic bacterial cells, suggesting that cell motility is linked to the pool of non-modified 1,3-diaminopropane. Indeed, deletion of dpa hinders biofilm formation and increases twitching motion confirming the impact of balancing the levels of 1,3-diaminopropane on cell motility. The crystal structure of Dpa reveals topological and functional differences from other bacterial polyamine acetyltransferases, adopting a β-swapped quaternary arrangement similar to that of eukaryotic polyamine acetyltransferases with a central size exclusion channel that sieves through the cellular polyamine pool. The structure of catalytically impaired Dpa(Y128F) in complex with the reaction product shows that binding and orientation of the polyamine substrates are conserved between different polyamine-acetyltransferases. |
format | Online Article Text |
id | pubmed-10267138 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-102671382023-06-15 A polyamine acetyltransferase regulates the motility and biofilm formation of Acinetobacter baumannii Armalytė, Julija Čepauskas, Albinas Šakalytė, Gabija Martinkus, Julius Skerniškytė, Jūratė Martens, Chloé Sužiedėlienė, Edita Garcia-Pino, Abel Jurėnas, Dukas Nat Commun Article Acinetobacter baumannii is a nosocomial pathogen highly resistant to environmental changes and antimicrobial treatments. Regulation of cellular motility and biofilm formation is important for its virulence, although it is poorly described at the molecular level. It has been previously reported that Acinetobacter genus specifically produces a small positively charged metabolite, polyamine 1,3-diaminopropane, that has been associated with cell motility and virulence. Here we show that A. baumannii encodes novel acetyltransferase, Dpa, that acetylates 1,3-diaminopropane, directly affecting the bacterium motility. Expression of dpa increases in bacteria that form pellicle and adhere to eukaryotic cells as compared to planktonic bacterial cells, suggesting that cell motility is linked to the pool of non-modified 1,3-diaminopropane. Indeed, deletion of dpa hinders biofilm formation and increases twitching motion confirming the impact of balancing the levels of 1,3-diaminopropane on cell motility. The crystal structure of Dpa reveals topological and functional differences from other bacterial polyamine acetyltransferases, adopting a β-swapped quaternary arrangement similar to that of eukaryotic polyamine acetyltransferases with a central size exclusion channel that sieves through the cellular polyamine pool. The structure of catalytically impaired Dpa(Y128F) in complex with the reaction product shows that binding and orientation of the polyamine substrates are conserved between different polyamine-acetyltransferases. Nature Publishing Group UK 2023-06-14 /pmc/articles/PMC10267138/ /pubmed/37316480 http://dx.doi.org/10.1038/s41467-023-39316-5 Text en © The Author(s) 2023 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 Armalytė, Julija Čepauskas, Albinas Šakalytė, Gabija Martinkus, Julius Skerniškytė, Jūratė Martens, Chloé Sužiedėlienė, Edita Garcia-Pino, Abel Jurėnas, Dukas A polyamine acetyltransferase regulates the motility and biofilm formation of Acinetobacter baumannii |
title | A polyamine acetyltransferase regulates the motility and biofilm formation of Acinetobacter baumannii |
title_full | A polyamine acetyltransferase regulates the motility and biofilm formation of Acinetobacter baumannii |
title_fullStr | A polyamine acetyltransferase regulates the motility and biofilm formation of Acinetobacter baumannii |
title_full_unstemmed | A polyamine acetyltransferase regulates the motility and biofilm formation of Acinetobacter baumannii |
title_short | A polyamine acetyltransferase regulates the motility and biofilm formation of Acinetobacter baumannii |
title_sort | polyamine acetyltransferase regulates the motility and biofilm formation of acinetobacter baumannii |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10267138/ https://www.ncbi.nlm.nih.gov/pubmed/37316480 http://dx.doi.org/10.1038/s41467-023-39316-5 |
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