Disulfide rearrangement triggered by translocon assembly controls lipopolysaccharide export

Shu Sin Chng, Mingyu Xue, Ronald A. Garner, Hiroshi Kadokura, Dana Boyd, Jonathan Beckwith, Daniel Kahne

Research output: Contribution to journalArticlepeer-review

80 Citations (Scopus)


The presence of lipopolysaccharide (LPS) on the cell surface of Gram-negative bacteria is critical for viability. A conserved b-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.

Original languageEnglish
Pages (from-to)1665-1668
Number of pages4
Issue number6102
Publication statusPublished - 2012 Sept 28


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