Murein (peptidoglycan) structure, architecture and biosynthesis in Escherichia coli |
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| Authors: | Waldemar Vollmer Ute Bertsche |
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| Institution: | a Institute for Cell and Molecular Biosciences, Medical School, University of Newcastle upon Tyne, Catherine Cookson Building, Framlington Place, Newcastle upon Tyne, NE2 4HH, UK
b Microbial Genetics, University of Tübingen, Tübingen, Germany |
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| Abstract: | The periplasmic murein (peptidoglycan) sacculus is a giant macromolecule made of glycan strands cross-linked by short peptides completely surrounding the cytoplasmic membrane to protect the cell from lysis due to its internal osmotic pressure. More than 50 different muropeptides are released from the sacculus by treatment with a muramidase. Escherichia coli has six murein synthases which enlarge the sacculus by transglycosylation and transpeptidation of lipid II precursor. A set of twelve periplasmic murein hydrolases (autolysins) release murein fragments during cell growth and division. Recent data on the in vitro murein synthesis activities of the murein synthases and on the interactions between murein synthases, hydrolases and cell cycle related proteins are being summarized. There are different models for the architecture of murein and for the incorporation of new precursor into the sacculus. We present a model in which morphogenesis of the rod-shaped E. coli is driven by cytoskeleton elements competing for the control over the murein synthesis multi-enzyme complexes. |
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| Keywords: | GlcNAc N-acetylglucosamine m-A2pm meso-diaminopimelic acid MurNAc N-acetylmuramic acid nPB non-Penicillin-binding domain PBP Penicillin-binding protein TG transglycosylase TP transpeptidase UDP uridyl diphosphate |
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