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- W2029884778 abstract "Autotransporter (AT) proteins are the largest class of extracellular virulence proteins secreted from Gram-negative bacteria. The mechanism by which AT proteins cross the bacterial outer membrane (OM), in the absence of ATP or another external energy source, is unknown. Here we demonstrate a linear correlation between localized regions of stability (ΔG(folding)) in the mature virulence protein (the AT passenger) and OM secretion efficiency. Destabilizing the C-terminal β-helical domain of a passenger reduced secretion efficiency. In contrast, destabilizing the globular N-terminal domain of a passenger produced a linearly correlated increase in secretion efficiency. Thus, C-terminal passenger stability facilitates OM secretion, whereas N-terminal stability hinders it. The contributions of regional passenger stability to OM secretion demonstrate a crucial role for the passenger itself in directing its secretion, suggesting a novel type of ATP-independent, folding-driven transporter." @default.
- W2029884778 created "2016-06-24" @default.
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- W2029884778 date "2012-02-01" @default.
- W2029884778 modified "2023-09-30" @default.
- W2029884778 title "ATP-Independent Control of Autotransporter Virulence Protein Transport via the Folding Properties of the Secreted Protein" @default.
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- W2029884778 doi "https://doi.org/10.1016/j.chembiol.2011.11.009" @default.
- W2029884778 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3288764" @default.
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