期刊
SCIENCE
卷 337, 期 6102, 页码 1665-1668出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1227215
关键词
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资金
- NIH [AI081059]
- NIGMS [41883]
- Japan Society for the Promotion of Science [21580092]
- Grants-in-Aid for Scientific Research [21580092] Funding Source: KAKEN
The presence of lipopolysaccharide (LPS) on the cell surface of Gram-negative bacteria is critical for viability. A conserved beta-barrel membrane protein LptD (lipopolysaccharide transport protein D) translocates LPS from the periplasm across the outer membrane (OM). In Escherichia coli, this protein contains two disulfide bonds and forms the OM LPS translocon with the lipoprotein LptE. Here, we identified seven in vivo states on the oxidative-folding pathway of LptD. Proper assembly involved a nonfunctional intermediate containing non-native disulfides. Intermediate formation required the oxidase DsbA, and subsequent maturation to the active form with native disulfides was triggered by LptE. Thus, disulfide bond-dependent protein folding of LptD requires the proper assembly of a two-protein complex to promote disulfide bond rearrangement.
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