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Characterization of the Shigella and Salmonella Type III Secretion System Tip–Translocon Protein–Protein Interaction by Paramagnetic Relaxation Enhancement
Author(s) -
Kaur Kawaljit,
Chatterjee Srirupa,
De Guzman Roberto N.
Publication year - 2016
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201500556
Subject(s) - translocon , type three secretion system , secretion , ectodomain , shigella flexneri , shigella , microbiology and biotechnology , chemistry , endoplasmic reticulum , secretory protein , salmonella , biophysics , biology , virulence , membrane protein , bacteria , biochemistry , escherichia coli , genetics , membrane , receptor , gene
Many Gram‐negative pathogens, such as Shigella and Salmonella , assemble the type III secretion system (T3SS) to inject virulence proteins directly into eukaryotic cells to initiate infectious diseases. The needle apparatus of the T3SS consists of a base, an extracellular needle, a tip protein complex, and a translocon. The atomic structure of the assembled tip complex and the translocon is unknown. Here, we show by NMR paramagnetic relaxation enhancement (PRE) that the mixed α–β domain at the distal region of the Shigella and Salmonella tip proteins interacts with the N‐terminal ectodomain of their major translocon proteins. Our results reveal the binding surfaces involved in the tip–translocon protein–protein interaction and provide insights about the assembly of the needle apparatus of the T3SS.