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New Insights into the Lpt Machinery for Lipopolysaccharide Transport to the Cell Surface: LptA-LptC Interaction and LptA Stability as Sensors of a Properly Assembled Transenvelope Complex
It is shown here that in vivo LptA and LptC physically interact, forming a stable complex, and, based on the analysis of loss-of-function mutations in LpsC, it is suggested that the C-terminal region of LPTC is implicated in LptB binding, and the recently proposed transenvelope model for LPS transport is supported.
The Escherichia coli Lpt Transenvelope Protein Complex for Lipopolysaccharide Export Is Assembled via Conserved Structurally Homologous Domains
It is shown that LptC lacking the transmembrane region is viable and can bind the LptBFG inner membrane complex and further support the model whereby the bridge connecting the inner and outer membranes would be based on the conserved structurally homologous jellyroll domain shared by five out of the seven Lpt components.
The lipopolysaccharide transport (Lpt) machinery: A nonconventional transporter for lipopolysaccharide assembly at the outer membrane of Gram-negative bacteria
This review focuses on LPS biogenesis and discusses recent advances that have contributed to the understanding of how this complex molecule is transported across the cellular envelope and is assembled at the OM outer leaflet.
Peptidoglycan Remodeling Enables Escherichia coli To Survive Severe Outer Membrane Assembly Defect
This work shows that Escherichia coli cells are capable of avoiding lysis when the transport of LPS to the OM is compromised, by utilizing LD-transpeptidases (LDTs) to generate 3-3 cross-links in the PG.
Copper inhibits peptidoglycan LD-transpeptidases suppressing β-lactam resistance due to bypass of penicillin-binding proteins
Copper inhibits peptidoglycan LD-transpeptidases, causing higher permeability in the outermembrane and precluding strains of Escherichia coli and Enterococcus faecium to utilize these enzymes in a bypass mechanism to achieve β-lactam resistance.
Functional Interaction between the Cytoplasmic ABC Protein LptB and the Inner Membrane LptC Protein, Components of the Lipopolysaccharide Transport Machinery in Escherichia coli
Increased expression of the membrane-associated ABC protein LptB can suppress defects of LptC, which participates in the formation of the periplasmic bridge, which reveals functional interactions between these two components and supports a role of LPTB in the assembly of the Lpt machine.