Cytoplasmic ATP hydrolysis powers transport of lipopolysaccharide across the periplasm in E. coli.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 23138981.
- Also identified by DOI 10.1126/science.1228984 and PMC identifier 3552488.
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Abstract
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.
Medical subject headings
- ATP-Binding Cassette Transporters
- ATP-Binding Cassette Transporters/chemistry
- ATP-Binding Cassette Transporters/metabolism
- Adenosine Triphosphate
- Adenosine Triphosphate/metabolism
- Bacterial Proteins
- Bacterial Proteins/chemistry
- Bacterial Proteins/metabolism
- Biological Transport
- Carrier Proteins
- Carrier Proteins/chemistry
- Carrier Proteins/genetics
- Carrier Proteins/metabolism
- Cytoplasm
- Cytoplasm/metabolism
- Escherichia coli
- Escherichia coli/metabolism
- Escherichia coli Proteins
- Escherichia coli Proteins/chemistry
- Escherichia coli Proteins/genetics
- Escherichia coli Proteins/metabolism
- Hydrolysis
- Lipopolysaccharides
- Lipopolysaccharides/metabolism
- Membrane Proteins
- Membrane Proteins/chemistry
- Membrane Proteins/genetics
- Membrane Proteins/metabolism
- Mutation
- Periplasm
- Periplasm/metabolism
- Protein Conformation