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PLoS Genet. 2014 Nov 13;10(11):e1004800. doi: 10.1371/journal.pgen.1004800. eCollection 2014.

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

Author information

1
Junior Research Group Infection Biology of Salmonella, Helmholtz Centre for Infection Research, Braunschweig, Germany.
2
Department of Biology, University of Utah, Salt Lake City, Utah, United States of America.

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.

PMID:
25393010
PMCID:
PMC4230889
DOI:
10.1371/journal.pgen.1004800
[Indexed for MEDLINE]
Free PMC Article
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