Dephosphorylated NPr of the nitrogen PTS regulates lipid A biosynthesis by direct interaction with LpxD |
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Authors: | Kim Hyun-Jin Lee Chang-Ro Kim Miri Peterkofsky Alan Seok Yeong-Jae |
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Affiliation: | aDepartment of Biological Sciences and Institute of Microbiology, Seoul National University, Seoul 151-742, Republic of Korea;bLaboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA;cDepartment of Biophysics and Chemical Biology, Seoul National University, Seoul 151-742, Republic of Korea |
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Abstract: | Bacterial phosphoenolpyruvate-dependent phosphotransferase systems (PTS) play multiple roles in addition to sugar transport. Recent studies revealed that enzyme IIANtr of the nitrogen PTS regulates the intracellular concentration of K+ by direct interaction with TrkA and KdpD. In this study, we show that dephosphorylated NPr of the nitrogen PTS interacts with Escherichia coli LpxD which catalyzes biosynthesis of lipid A of the lipopolysaccharide (LPS) layer. Mutations in lipid A biosynthetic genes such as lpxD are known to confer hypersensitivity to hydrophobic antibiotics such as rifampin; a ptsO (encoding NPr) deletion mutant showed increased resistance to rifampin and increased LPS biosynthesis. Taken together, our data suggest that unphosphorylated NPr decreases lipid A biosynthesis by inhibiting LpxD activity. |
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Keywords: | Escherichia coli Lipid A Nitrogen PTS NPr Protein-protein interaction |
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