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Disulfide rearrangement triggered by translocon assembly controls lipopolysaccharide export.

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

SUBMITTER: Chng SS

PROVIDER: S-EPMC3489181 | biostudies-literature | 2012 Sep

REPOSITORIES: biostudies-literature

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Disulfide rearrangement triggered by translocon assembly controls lipopolysaccharide export.

Chng Shu-Sin SS Xue Mingyu M Garner Ronald A RA Kadokura Hiroshi H Boyd Dana D Beckwith Jonathan J Kahne Daniel D

Science (New York, N.Y.) 20120830 6102

The presence of lipopolysaccharide (LPS) on the cell surface of Gram-negative bacteria is critical for viability. A conserved β-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 no ...[more]

PMID: 22936569

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