Interactions between late-acting proteins required for peptidoglycan synthesis during sporulation. SEDS proteins are a widespread family of bacterial cell wall polymerases. MurJ is the flippase of lipid-linked precursors for peptidoglycan biogenesis. Growth of Escherichia coli: significance of peptidoglycan degradation during elongation and septation. Beta-lactam antibiotics induce a lethal malfunctioning of the bacterial cell wall synthesis machinery. Role of class A penicillin-binding proteins in the expression of beta-lactam resistance in Enterococcus faecium. Peptidoglycan synthesis in the absence of class A penicillin-binding proteins in Bacillus subtilis. The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis. Sauvage, E., Kerff, F., Terrak, M., Ayala, J. Mutational analysis of the Streptococcus pneumoniae bimodular class A penicillin-binding proteins. Gene disruption studies of penicillin-binding proteins 1a, 1b, and 2a in Streptococcus pneumoniae. Lysis of Escherichia coli by beta-lactam antibiotics: deletion analysis of the role of penicillin-binding proteins 1A and 1B. FtsZ ring structure associated with division in Escherichia coli. Rod-like bacterial shape is maintained by feedback between cell curvature and cytoskeletal localization. The bacterial actin MreB rotates, and rotation depends on cell-wall assembly. Processive movement of MreB-associated cell wall biosynthetic complexes in bacteria. Coupled, circumferential motions of the cell wall synthesis machinery and MreB filaments in B. Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis. From the regulation of peptidoglycan synthesis to bacterial growth and morphology. These findings thus necessitate a fundamental change in our conception of the cell wall assembly process in bacteria. Instead, our results indicate that cell wall synthesis is mediated by two distinct polymerase systems, shape, elongation, division, sporulation (SEDS)-family proteins working within the cytoskeletal machines and aPBP enzymes functioning outside these complexes. We find that aPBP activity is not necessary for glycan polymerization by the cell elongation machinery, as is commonly believed. Here, we use an in vivo cell wall polymerase assay in Escherichia coli combined with measurements of the localization dynamics of synthesis proteins to investigate this hypothesis.
Current models of the wall assembly mechanism assume that class A penicillin-binding proteins (aPBPs), the targets of penicillin-like drugs, function as the primary cell wall polymerases within these machineries. Multi-protein complexes organized by cytoskeletal proteins are essential for cell wall biogenesis in most bacteria.
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