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Disulfide Rearrangement Triggered by Translocon Assembly Controls Lipopolysaccharide Export
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Disulfide Rearrangement Triggered by Translocon Assembly Controls Lipopolysaccharide Export
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Journal Article
Disulfide Rearrangement Triggered by Translocon Assembly Controls Lipopolysaccharide Export
2012
Overview
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 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.
Publisher
American Association for the Advancement of Science,The American Association for the Advancement of Science
Subject
/ Analytical, structural and metabolic biochemistry
/ Assembly
/ Bacteria
/ Bacterial Outer Membrane Proteins - chemistry
/ Bacterial Outer Membrane Proteins - genetics
/ Bacterial Outer Membrane Proteins - metabolism
/ Biological and medical sciences
/ Cells
/ E coli
/ Escherichia coli - metabolism
/ Escherichia coli Proteins - chemistry
/ Escherichia coli Proteins - genetics
/ Escherichia coli Proteins - metabolism
/ Exports
/ Folding
/ Fundamental and applied biological sciences. Psychology
/ Lipopolysaccharides - metabolism
/ Molecular and cellular biology
/ Pathways
/ Protein Disulfide-Isomerases - metabolism
/ Protein Structure, Secondary
/ Proteins
/ Sulfides
