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FEBS Lett. 2019 Sep 4. doi: 10.1002/1873-3468.13593. [Epub ahead of print]

Deciphering the specific interaction between the acyl carrier protein IacP and the T3SS-major hydrophobic translocator SipB from Salmonella.

Author information

1
LISM, Institut de Microbiologie de la Méditerranée, CNRS and Aix-Marseille Univ., Marseille, France.
2
NMR Platform, Institut de Microbiologie de la Méditerranée, CNRS and Aix-Marseille Univ., Marseille, France.
3
Proteomics Platform- IBISA2, Institut de Microbiologie de la Méditerranée, CNRS and Aix-Marseille Univ., Marseille, France.

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'-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. This article is protected by copyright. All rights reserved.

KEYWORDS:

ACP ; Salmonella ; IacP; SPI 1; SipB; acyl carrier protein; acylation; protein-protein interaction; translocator; translocon; type 3 secretion system

PMID:
31486064
DOI:
10.1002/1873-3468.13593

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