PMID:9139895
| Citation |
de Pedro, MA, Quintela, JC, Höltje, JV and Schwarz, H (1997) Murein segregation in Escherichia coli. J. Bacteriol. 179:2823-34 |
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| Abstract |
Peptidoglycan (murein) segregation has been studied by means of a new labeling method. The method relies on the ability of Escherichia coli cells to incorporate D-Cys into macromolecular murein. The incorporation depends on a periplasmic amino acid exchange reaction. At low concentrations, D-Cys is innocuous to the cell. The distribution of modified murein in purified sacculi can be traced and visualized by immunodetection of the -SH groups by fluorescence and electron microscopy techniques. Analysis of murein segregation in wild-type and cell division mutant strains revealed that murein in polar caps is metabolically inert and is segregated in a conservative fashion. Elongation of the sacculus apparently occurs by diffuse insertion of precursors over the cylindrical part of the cell surface. At the initiation of cell division, there is a FtsZ-dependent localized activation of murein synthesis at the potential division sites. Penicillin-binding protein 3 and the products of the division genes ftsA and ftsQ are dispensable for the activation of division sites. As a consequence, under restrictive conditions ftsA,ftsI,or ftsQ mutants generate filamentous sacculi with rings of all-new murein at the positions where septa would otherwise develop. |
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| Keywords |
Bacterial Proteins/metabolism; Carrier Proteins; Cell Division; Cell Fractionation; Cysteine/metabolism; Cytoskeletal Proteins; Escherichia coli/genetics; Escherichia coli/physiology; Escherichia coli/ultrastructure; Escherichia coli Proteins; GTP-Binding Proteins/metabolism; Genes, Bacterial; Hexosyltransferases/metabolism; Membrane Proteins/metabolism; Microscopy, Immunoelectron; Multienzyme Complexes/metabolism; Muramoylpentapeptide Carboxypeptidase; Penicillin-Binding Proteins; Peptidoglycan/biosynthesis; Peptidoglycan Glycosyltransferase; Peptidyl Transferases/metabolism; Stereoisomerism |
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