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dc.contributor.authorErhardt, Marc
dc.contributor.authorMertens, Max E
dc.contributor.authorFabiani, Florian D
dc.contributor.authorHughes, Kelly T
dc.date.accessioned2014-12-16T10:34:21Z
dc.date.available2014-12-16T10:34:21Z
dc.date.issued2014-11
dc.identifier.citationATPase-Independent Type-III Protein Secretion in Salmonella enterica. 2014, 10 (11):e1004800 PLoS Genet.en
dc.identifier.issn1553-7404
dc.identifier.pmid25393010
dc.identifier.doi10.1371/journal.pgen.1004800
dc.identifier.urihttp://hdl.handle.net/10033/337216
dc.description.abstractType-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.
dc.language.isoenen
dc.titleATPase-Independent Type-III Protein Secretion in Salmonella enterica.en
dc.typeArticleen
dc.identifier.journalPLoS geneticsen
refterms.dateFOA2018-06-13T02:22:27Z
html.description.abstractType-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.


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