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Trends Microbiol. 2015 May;23(5):296-300. doi: 10.1016/j.tim.2015.01.012. Epub 2015 Feb 17.

Fueling type III secretion.

Author information

1
Cell Biology and Metabolism Program, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.
2
Department of Molecular Biology and Microbiology, Case Western Reserve University, Cleveland, OH 44106-4960, USA. Electronic address: arne.rietsch@case.edu.

Abstract

Type III secretion systems (T3SSs) are complex nanomachines that export proteins from the bacterial cytoplasm across the cell envelope in a single step. They are at the core of the machinery used to assemble the bacterial flagellum, and the needle complex many Gram-negative pathogens use to inject effector proteins into host cells and cause disease. Several models have been put forward to explain how this export is energized, and the mechanism has been the subject of considerable debate. Here we present an overview of these models and discuss their relative merits. Recent evidence suggests that the proton motive force (pmf) is the primary energy source for type III secretion, although contribution from refolding of secreted proteins has not been ruled out. The mechanism by which the pmf is converted to protein export remains enigmatic.

KEYWORDS:

ATPase; T3SS; flagellum; needle complex; proton motive force

PMID:
25701111
PMCID:
PMC4417389
DOI:
10.1016/j.tim.2015.01.012
[Indexed for MEDLINE]
Free PMC Article
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