Journal
SCIENCE
Volume 338, Issue 6111, Pages 1214-1217Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1228984
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Funding
- NIH [AI081059, GM066174]
- Fannie and John Hertz Foundation
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Millions of molecules of lipopolysaccharide (LPS) must be assembled on the Escherichia coli cell surface each time the cell divides. The biogenesis of LPS requires seven essential lipopolysaccharide transport (Lpt) proteins to move LPS from the inner membrane through the periplasm to the cell surface. However, no intermediate transport states have been observed. We developed methods to observe intermediate LPS molecules bound to Lpt proteins in the process of being transported in vivo. Movement of individual LPS molecules along these binding sites required multiple rounds of adenosine triphosphate (ATP) hydrolysis in vitro, which suggests that ATP is used to push a continuous stream of LPS through a transenvelope bridge in discrete steps against a concentration gradient.
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