Deciphering the specific interaction between the acyl carrier protein IacP and the T3SS‐major hydrophobic translocator SipB from Salmonella - Aix-Marseille Université Accéder directement au contenu
Article Dans Une Revue FEBS Letters Année : 2019

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 0-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.
Fichier principal
Vignette du fichier
Canestrari_FEBS_2019_Total.pdf (5.14 Mo) Télécharger le fichier
Origine : Fichiers produits par l'(les) auteur(s)

Dates et versions

hal-03173717 , version 1 (18-03-2021)

Identifiants

Citer

Mickaël J Canestrari, Bastien Serrano, Julia Bartoli, Valérie Prima, Olivier Bornet, et al.. Deciphering the specific interaction between the acyl carrier protein IacP and the T3SS‐major hydrophobic translocator SipB from Salmonella. FEBS Letters, 2019, 594, pp.251 - 265. ⟨10.1002/1873-3468.13593⟩. ⟨hal-03173717⟩
52 Consultations
129 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More