A polyamine acetyltransferase regulates the motility and biofilm formation of Acinetobacter baumannii

Julija Armalytė, Albinas Čepauskas, Gabija Šakalytė, Julius Martinkus, Jūratė Skerniškytė, Chloé Martens, Edita Sužiedėlienė, Abel Garcia-Pino () and Dukas Jurėnas ()
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Julija Armalytė: Vilnius University
Albinas Čepauskas: Vilnius University
Gabija Šakalytė: Vilnius University
Julius Martinkus: Vilnius University
Jūratė Skerniškytė: Vilnius University
Chloé Martens: Université Libre de Bruxelles (ULB), Bruxelles, Belgium. Building BC, Boulevard du Triomphe
Edita Sužiedėlienė: Vilnius University
Abel Garcia-Pino: Université Libre de Bruxelles (ULB), Building BC, Room 1C4 203, Boulevard du Triomphe
Dukas Jurėnas: Vilnius University

Nature Communications, 2023, vol. 14, issue 1, 1-11

Abstract: Abstract 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 DpaY128F in complex with the reaction product shows that binding and orientation of the polyamine substrates are conserved between different polyamine-acetyltransferases.

Date: 2023
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DOI: 10.1038/s41467-023-39316-5

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