Genetically distinct pathways guide effector export through the type VI secretion system.

Abstract:

:Bacterial secretion systems often employ molecular chaperones to recognize and facilitate export of their substrates. Recent work demonstrated that a secreted component of the type VI secretion system (T6SS), haemolysin co-regulated protein (Hcp), binds directly to effectors, enhancing their stability in the bacterial cytoplasm. Herein, we describe a quantitative cellular proteomics screen for T6S substrates that exploits this chaperone-like quality of Hcp. Application of this approach to the Hcp secretion island I-encoded T6SS (H1-T6SS) of Pseudomonas aeruginosa led to the identification of a novel effector protein, termed Tse4 (type VI secretion exported 4), subsequently shown to act as a potent intra-specific H1-T6SS-delivered antibacterial toxin. Interestingly, our screen failed to identify two predicted H1-T6SS effectors, Tse5 and Tse6, which differ from Hcp-stabilized substrates by the presence of toxin-associated PAAR-repeat motifs and genetic linkage to members of the valine-glycine repeat protein G (vgrG) genes. Genetic studies further distinguished these two groups of effectors: Hcp-stabilized effectors were found to display redundancy in interbacterial competition with respect to the requirement for the two H1-T6SS-exported VgrG proteins, whereas Tse5 and Tse6 delivery strictly required a cognate VgrG. Together, we propose that interaction with either VgrG or Hcp defines distinct pathways for T6S effector export.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Whitney JC,Beck CM,Goo YA,Russell AB,Harding BN,De Leon JA,Cunningham DA,Tran BQ,Low DA,Goodlett DR,Hayes CS,Mougous JD

doi

10.1111/mmi.12571

subject

Has Abstract

pub_date

2014-05-01 00:00:00

pages

529-42

issue

3

eissn

0950-382X

issn

1365-2958

journal_volume

92

pub_type

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