ATPase-independent type-III protein secretion in Salmonella enterica.

Abstract:

:Type-III protein secretion systems are utilized by gram-negative pathogens to secrete building blocks of the bacterial flagellum, virulence effectors from the cytoplasm into host cells, and structural subunits of the needle complex. The flagellar type-III secretion apparatus utilizes both the energy of the proton motive force and ATP hydrolysis to energize substrate unfolding and translocation. We report formation of functional flagella in the absence of type-III ATPase activity by mutations that increased the proton motive force and flagellar substrate levels. We additionally show that increased proton motive force bypassed the requirement of the Salmonella pathogenicity island 1 virulence-associated type-III ATPase for secretion. Our data support a role for type-III ATPases in enhancing secretion efficiency under limited secretion substrate concentrations and reveal the dispensability of ATPase activity in the type-III protein export process.

journal_name

PLoS Genet

journal_title

PLoS genetics

authors

Erhardt M,Mertens ME,Fabiani FD,Hughes KT

doi

10.1371/journal.pgen.1004800

subject

Has Abstract

pub_date

2014-11-13 00:00:00

pages

e1004800

issue

11

eissn

1553-7390

issn

1553-7404

pii

PGENETICS-D-14-01838

journal_volume

10

pub_type

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