PXD018859

PXD018859 is an original dataset announced via ProteomeXchange.

Title	Selection of the length of fatty acyl chain and of the acylation site by the acyltransferase governs activation of RTX toxins
Description	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 acylation on ε-amino groups of two internal conserved lysine residues by co-expressed toxin-activating acyltransferases. We investigated how the chemical nature, position and number of bound acyl chains govern the activities of Bordetella pertussis adenylate cyclase toxin (CyaA), Escherichia coli α-hemolysin (HlyA) and Kingella kingae cytotoxin (RtxA). The three protoxins were acylated in the same E. coli cell background by either of the CyaC, HlyC and RtxC acyltransferases. The results revealed that the acyltransferase itself selects from the acyl-ACP pool of the producing bacterium the type of the acyl chain of adapted length to be covalently linked to the protoxin. The acyltransferase also selects whether both or only one of two conserved lysine residues of the protoxin will be posttranslationally acylated. Functional assays then revealed that RtxA has to be modified by 14-carbon fatty acyl chains to be biologically active, while HlyA remains active also when modified by 16-carbon acyl chains and CyaA is activated exclusively by 16-carbon acyl chains. These results suggest a structural adaptation of the toxin molecules to the length of the acyl chains used for modification of their crucial acylated lysine residue in the second, more conserved acylation site
HostingRepository	PRIDE
AnnounceDate	2020-05-20
AnnouncementXML	Submission_2020-08-11_05:41:15.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	David Jurnečka
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562; scientific name: Bordetella pertussis Tohama I; NCBI TaxID: 257313;
ModificationList	palmitoylated residue; myristoylated residue; monohydroxylated residue
Instrument	Bruker Daltonics solarix series

Revision	Datetime	Status	ChangeLog Entry
0	2020-04-28 08:24:05	ID requested
1	2020-05-19 23:02:08	announced
⏵ 2	2020-08-11 05:41:15	announced	2020-08-11: Updated publication reference for PubMed record(s): 32461253.

Osickova A, Khaliq H, Masin J, Jurnecka D, Sukova A, Fiser R, Holubova J, Stanek O, Sebo P, Osicka R, Acyltransferase-mediated selection of the length of the fatty acyl chain and of the acylation site governs activation of bacterial RTX toxins. J Biol Chem, 295(28):9268-9280(2020) [pubmed]

submitter keyword: acylation, acyltransferase, cytotoxicity, fatty acyl, RTX toxin

Prof. Peter Sebo, PhD.
contact affiliation	Institute of Microbiology of the CAS, v. v. i.
contact email	sebo@biomed.cas.cz
lab head
David Jurnečka
contact affiliation	Institute of Microbiology, Czech Academy of Sciences
contact email	david.jurnecka@biomed.cas.cz
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD018859
     1. Label: PRIDE project
     2. Name: Selection of the length of fatty acyl chain and of the acylation site by the acyltransferase governs activation of RTX toxins