Deciphering the specific interaction between the acyl carrier protein IacP and the T3SS‐major hydrophobic translocator SipB from Salmonella
Résumé
Salmonella is a facultative intracellular pathogen that invades epithelial cells of the intestine using the SPI-1 Type 3 secretion System (T3SS). Insertion of the SPI-1 T3SS translocon is facilitated by acylation of the translocator SipB, which involves a protein-protein interaction with the acyl carrier protein IacP. Using nuclear magnetic resonance and biological tests, we identified the residues of IacP that are involved in the interaction with SipB. Our results suggest that the 4'-phosphopantetheine group that functionalizes IacP participates in the interaction. Its solvent exposition may rely on two residues highly conserved in acyl carrier proteins associated with T3SS. This study is the first to address the specificity of acyl carrier proteins associated with T3SS.
Mots clés
ACP
acyl carrier protein
type 3 secretion system
translocon
translocator
protein-protein interaction
acylation
Salmonella
SPI 1
IacP
SipB
ACP Abbreviations used: SPI-1
Salmonella pathogenicity island 1
T3SS
4¢-PP
4¢-phosphopantetheine
HSQC
heteronuclear single quantum coherence
pfe
Pseudomonas fluorescens
sfl
Shigella flexneri
stm
Salmonella Typhimurium
Domaines
BactériologieOrigine | Fichiers produits par l'(les) auteur(s) |
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