Murein segregation in Escherichia coli
| Autor: | J V Höltje, José Carlos Quintela, H Schwarz, M A de Pedro |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
Peptidoglycan glycosyltransferase
Cell division Mutant Periplasmic space biochemical phenomena metabolism and nutrition Biology medicine.disease_cause Microbiology carbohydrates (lipids) chemistry.chemical_compound chemistry Biochemistry medicine Biophysics bacteria Peptidoglycan FtsA Cytoskeleton Molecular Biology Escherichia coli Research Article |
| Zdroj: | Journal of Bacteriology. 179:2823-2834 |
| ISSN: | 1098-5530 0021-9193 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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