Journal
SCIENCE
Volume 359, Issue 6377, Pages 798-+Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aar1886
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Funding
- National Science Foundation Graduate Research Fellowship
- Kavli Institute for Bionano Science and Technology at Harvard University
- Blavatnik Biomedical Accelerator at Harvard University
- National Science Foundation [DMR-0820484]
- National Institute of Allergy and Infectious Diseases [AI081059, AI109764]
- National Institute of General Medical Sciences [GM066174]
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [U19AI109764, R01AI081059] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM066174] Funding Source: NIH RePORTER
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Gram-negative bacteria have an outer membrane that serves as a barrier to noxious agents in the environment. This protective function is dependent on lipopolysaccharide, a large glycolipid located in the outer leaflet of the outer membrane. Lipopolysaccharide is synthesized at the cytoplasmic membrane and must be transported to the cell surface. To understand this transport process, we reconstituted membrane-to-membrane movement of lipopolysaccharide by incorporating purified inner and outer membrane transport complexes into separate proteoliposomes. Transport involved stable association between the inner and outer membrane proteoliposomes. Our results support a model in which lipopolysaccharide molecules are pushed one after the other in a PEZ dispenser-like manner across a protein bridge that connects the inner and outer membranes.
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