![]() ![]() Using fluorescent vancomycin staining in B. Control of cell morphogenesis in bacteria: two distinct ways to make a rod-shaped cell. Insertion and fate of the cell wall in Bacillus subtilis. crescentus and as an intermediate filament-like protein. Presents crescentin as a cell shape determinant in C. The bacterial cytoskeleton: an intermediate filament-like function in cell shape. Division site selection in Escherichia coli involves dynamic redistribution of Min proteins within coiled structures that extend between the two cell poles. MreB, the cell shape-determining bacterial actin homologue, co-ordinates cell wall morphogenesis in Caulobacter crescentus. Dysfunctional MreB inhibits chromosome segregation in Escherichia coli. ![]() Kruse, T., Møller-Jensen, J., Løbner-Olesen, A. An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins. subtilis cells, indicating a cytoskeletal function.īork, P., Sander, C. Reveals the helical structures formed by MreB and Mbl within B. Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis. Shows the X-ray crystal structure of MreB as well as its in vitro filament formation, comparing it to actin. Prokaryotic origin of the actin cytoskeleton. Characterization and genetic analysis of a mutant of Escherichia coli K-12 with rounded morphology. The divIVB region of the Bacillus subtilis chromosome encodes homologs of Escherichia coli septum placement ( minCD) and cell shape ( mreBCD) determinants. Mutant isolation and molecular cloning of mre genes, which determine cell shape, sensitivity to mecillinam, and amount of penicillin-binding proteins in Escherichia coli. Identification of the MreB protein and its gene sequence, connecting it with cell-shape determination. Determinations of the DNA sequence of the mreB gene and of the gene products of the mre region that function in formation of the rod shape of Escherichia coli cells. Identification of Bacillus subtilis genes for septum placement and shape determination. Role and expression of the Bacillus subtilis rodC operon. The isolation and characterization of mutants of Bacillus subtilis and Bacillus licheniformis with disturbed morphology and cell division. Mapping of rod mutants of Bacillus subtilis. Endopeptidase penicillin-binding proteins 4 and 7 play auxiliary roles in determining uniform morphology of Escherichia coli. Penicillin binding protein 5 affects cell diameter, contour, and morphology of Escherichia coli. Cluster of mrdA and mrdB genes responsible for the rod shape and mecillinam sensitivity of Escherichia coli. Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12. Morphogenetic aspects of murein structure and biosynthesis. The rigid layer of the cell wall of Escherichia coli strain B. The first comprehensive review of the bacterial cell wall, this paper introduced now-standard nomenclature such as 'murein' and 'sacculus'. Bagshaped macromolecules - a new outlook on bacterial cell walls. Bacterial protoplasts induced by penicillin. The isolation of protoplasts from Bacillus megaterium by controlled treatment with lysozyme. These proteins form internal structures within cells at locations where they are thought to influence peptidoglycan synthesis or remodelling.įuture research on the nature of the peptidoglycan synthesis machinery and its relationship with the bacterial cytoskeleton is key to our understanding of cell-shape generation. FtsZ is essential for cell division, MreB is a rod shape determinant and crescentin is required for the curved-rod shape of Caulobacter crescentus. ![]() These regions of localized peptidoglycan synthesis vary among bacteria and often change during the cell cycle, reflecting different modes of cell growth (longitudinal, septal or polar).īacteria have counterparts of all three eukaryotic cytoskeletal protein classes: FtsZ for tubulin, MreB for actin and crescentin for intermediate filament proteins. Growth of the cell wall is not uniform, but is localized to specific regions. Different PBPs have specific roles in cell division and elongation, and therefore in cell-shape determination. The penicillin-binding proteins (PBPs) carry out the reactions for synthesis and remodelling of peptidoglycan. The bacterial cell wall, with its peptidoglycan layer, has a primary role in maintaining cell shape. Our understanding of bacterial cell shape has taken steps forward with the recent discovery of cytoskeletal elements such as cell-shape determinants, but there is still much to learn about how shape is generated and maintained. ![]()
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