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

被引:12
|
作者
Armalyte, Julija [1 ]
Cepauskas, Albinas [1 ,2 ]
Sakalyte, Gabija [1 ]
Martinkus, Julius [1 ]
Skerniskyte, Jurate [1 ]
Martens, Chloe [3 ]
Suziedeliene, Edita [1 ]
Garcia-Pino, Abel [2 ]
Jurenas, Dukas [1 ,4 ]
机构
[1] Vilnius Univ, Inst Biosci, Life Sci Ctr, Sauletekio Ave 7, LT-10257 Vilnius, Lithuania
[2] Univ Libre Bruxelles ULB, Fac Sci, Cellular & Mol Microbiol, Bldg BC,Room1C4 203,Blvd Triomphe, B-1050 Brussels, Belgium
[3] Univ Libre Bruxelles ULB, Ctr Struct Biol & Bioinformat, Bldg BC,Blvd Triomphe, B-1050 Brussels, Belgium
[4] Univ Libre Bruxelles ULB, Fac Sci, Lab Genet & Physiol Bacterienne, 12 Rue Profs Jeener & Brachet, B-6041 Gosselies, Belgium
基金
欧洲研究理事会;
关键词
SURFACE-ASSOCIATED MOTILITY; SPERMIDINE/SPERMINE N-1-ACETYLTRANSFERASE; HISTONE ACETYLTRANSFERASE; CRYSTAL-STRUCTURE; GNAT SUPERFAMILY; ACETYLATION; GENE; IDENTIFICATION; REFINEMENT; MUTANT;
D O I
10.1038/s41467-023-39316-5
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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 beta-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. Acinetobacter baumanii has an uncharacterized surface-associated motility which is a feature of its persistence. Here, Armalyte et al identify an acetyltransferase that affects this motility and present a functional and structural characterisation of it
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页数:11
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