Functionally essential interaction between Yersinia YscO and the T3S4 domain of YscP.

Abstract:

:The type III secretion (T3S) system is essential to the virulence of a large number of Gram-negative bacterial pathogens, including Yersinia. YscO is required for T3S in Yersinia and is known to interact with several other T3S proteins, including the chaperone SycD and the needle length regulator YscP. To define which interactions of YscO are required for T3S, we pursued model-guided mutagenesis: three conserved and surface-exposed regions of modeled YscO were targeted for multiple alanine substitutions. Most of the mutations abrogated T3S and did so in a recessive manner, consistent with a loss of function. Both functional and nonfunctional YscO mutant proteins interacted with SycD, indicating that the mutations had not affected protein stability. Likewise, both functional and nonfunctional versions of YscO were exclusively intrabacterial. Functional and nonfunctional versions of YscO were, however, distinguishable with respect to interaction with YscP. This interaction was observed only for wild-type YscO and a T3S-proficient mutant of YscO but not for the several T3S-deficient mutants of YscO. Evidence is presented that the YscO-YscP interaction is direct and that the type III secretion substrate specificity switch (T3S4) domain of YscP is sufficient for this interaction. These results provide evidence that the interaction of YscO with YscP, and in particular the T3S4 domain of YscP, is essential to type III secretion.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Mukerjea R,Ghosh P

doi

10.1128/JB.00876-13

subject

Has Abstract

pub_date

2013-10-01 00:00:00

pages

4631-8

issue

20

eissn

0021-9193

issn

1098-5530

pii

JB.00876-13

journal_volume

195

pub_type

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