期刊
CHEMISTRY & BIOLOGY
卷 19, 期 2, 页码 287-296出版社
CELL PRESS
DOI: 10.1016/j.chembiol.2011.11.009
关键词
-
资金
- NSF [MCB 0237945]
- NIH [T32 GM075762]
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 (Delta G(folding)) in the mature virulence protein (the AT passenger) and OM secretion efficiency. Destabilizing the C-terminal beta-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.
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