The Role of the Small Export Apparatus Protein, SctS, in the Activity of the Type III Secretion System

Overview

Journal Front Microbiol

Specialty Microbiology

Date 2019 Dec 5

PMID 31798543

Citations 5

Authors

Irit Tseytin

Bosko Mitrovic

Nofar David

Katja Langenfeld

Raz Zarivach

Andreas Diepold

Neta Sal-Man

Affiliations

Soon will be listed here.

Abstract

Many gram-negative pathogens utilize a protein complex, termed the type III secretion system (T3SS), to inject virulence factors from their cytoplasm directly into the host cell. An export apparatus that is formed by five putative integral membrane proteins (SctR/S/T/U/V), resides at the center of the T3SS complex. In this study, we characterized the smallest export apparatus protein, SctS, which contains two putative transmembrane domains (PTMD) that dynamically extract from the inner membrane and adopt a helix-turn-helix structure upon assembly of the T3SS. Replacement of each SctS PTMD with an alternative hydrophobic sequence resulted in abolishment of the T3SS activity, yet SctS self- and hetero-interactions as well as the overall assembly of the T3SS complex were unaffected. Our findings suggest that SctS PTMDs are not crucial for the interactions or the assembly of the T3SS base complex but rather that they are involved in adjusting the orientation of the export apparatus relative to additional T3SS sub-structures, such as the cytoplasmic- and the inner-membrane rings. This ensures the fittings between the dynamic and static components of the T3SS and supports the functionality of the T3SS complex.

Citing Articles

Secretion of functional interferon by the type 3 secretion system of enteropathogenic Escherichia coli.

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Interactions and substrate selectivity within the SctRST complex of the type III secretion system of enteropathogenic .

Tseytin I, Lezerovich S, David N, Sal-Man N Gut Microbes. 2021; 14(1):2013763.

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The Role of the Membrane-Associated Domain of the Export Apparatus Protein, EscV (SctV), in the Activity of the Type III Secretion System.

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