Deciphering the specific interaction between the acyl carrier protein IacP and the T3SS‐major hydrophobic translocator SipB from Salmonella
Abstract
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.
Keywords
ACP
acylation
protein-protein interaction
Salmonella pathogenicity Island 1
translocon
type 3 secretion system
acyl carrier protein
translocator
proteinprotein interaction
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
Domains
Life Sciences [q-bio]
Origin : Files produced by the author(s)