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ProteomicsSelection of the length of fatty acyl chain and of the acylation site by the acyltransferase governs activation of RTX toxins
Numerous proteins synthesized in cells ranging from bacteria to humans have to be posttranslationally acylated to become biologically active. Bacterial Repeats in ToXin (RTX) cytolysins form a prominent group of proteins that are synthesized as inactive protoxins and undergo a posttranslational acyl...
ORGANISM(S): Escherichia coli Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251) 
2020-05-20 | PXD018859 | Pride
Fatty acyl Rtx toxin Acyltransferase Acylation Cytotoxicity 
ProteomicsBioorthogonal Click Chemistry for Antibody-Free Profiling of Acetylation, Propionylation, and Butyrylation in Pseudomonas aeruginosa and Methicillin-Resistant Staphylococcus aureus
Lysine acylation is a post-translational modification (PTM) conserved in all domains of life and is essential for regulating diverse biological processes. Traditional methods for investigating acylation rely on anti-acyl-lysine-antibodies, which are costly, time-consuming, and often exhibit variable...
ORGANISM(S): Pseudomonas aeruginosa (strain UCBPP-PA14) Staphylococcus aureus 
2026-06-11 | PXD072564 | Pride
Butyrylation Propionylation Posttranslational modifications Acetylation Bacterial acylation 
UnknownProtein N-terminal acylation: An emerging field in bacterial cell physiology.
Not available
S-EPMC10062008 | biostudies-literature
UnknownGlycine acylation and trafficking of a new class of bacterial lipoprotein by a composite secretion system.
Not available
S-EPMC7943197 | biostudies-literature
UnknownA family of bacterial cysteine protease type III effectors utilizes acylation-dependent and -independent strategies to localize to plasma membranes.
Not available
S-EPMC2708883 | biostudies-literature
UnknownLysine Fatty Acylation: Regulatory Enzymes, Research Tools, and Biological Function.
Not available
S-EPMC8339906 | biostudies-literature
UnknownSite-specific acylation of a bacterial virulence regulator attenuates infection.
Not available
S-EPMC8439376 | biostudies-literature
UnknownAcyltransferase-mediated selection of the length of the fatty acyl chain and of the acylation site governs activation of bacterial RTX toxins.
Not available
S-EPMC7363117 | biostudies-literature
UnknownThe acylation state of surface lipoproteins of mollicute Acholeplasma laidlawii.
Not available
S-EPMC3123044 | biostudies-literature
ProteomicsResidues 1 to 563 of α-hemolysin alone form a fully functional pore and their proper membrane insertion depends on the acylation status of the molecule
The acylated pore-forming Repeats in ToXin (RTX) cytolysins α-hemolysin (HlyA) and adenylate cyclase toxin (CyaA) bind primarily to β2 integrins of leukocytes. HlyA binds the common CD18 subunit of the β2 integrins and CyaA selectively binds the CD11b subunit of complement receptor 3 (CR3). However,...
ORGANISM(S): Escherichia coli 
2024-03-25 | PXD046160 | Pride
Acylation Rtx toxin 
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