Does PBP2 Regulate Cell Division in E. coli?
Although penicillin has not made war humane, it probably saved over a million lives during World War II. The action of penicillin and related β-lactam antibiotics was early recognized to be extrmely broad, affecting the vast majority of bacterial species, and at the same time highly specific, generally producing little effect on eukaryotic cells. As the complex structure of the bacterial cell wall became known, the mechanism of action of β-lactams was also revealed: they bind covalently to the PBPs (‘penicillin binding proteins’), a set of integral membrane proteins which catalyse the terminal steps in the synthesis of the rigid peptoglycan wall (for review see Waxman and Strominger, 1983; Ghuysen, 1991).
KeywordsWild Type Strain Glycan Chain Muramic Acid Peptidoglycan Synthesis Transpeptidase Activity
Unable to display preview. Download preview PDF.
- Begg, K.J., Takasuga, A., Edwards, D.H., Edwards, J., Edwards, D.S., Spratt, B.G., Adachi, H., Ohta, T., Matsuzawa, H. and Donachie, W.D. (1990) The balance between different peptidoglycan precursors determines whether Escherichia coli cells will elongate or divide. J. Bacteriol. 172, 6697–6708.PubMedGoogle Scholar
- Broome-Smith, J.K. (1985) Construction of a mutant of Escherichia coli that has deletions of both the penicillin-binding protein 5 and 6 genes. J. Gen. Microbiol. 331, 2115–2118.Google Scholar
- del Portillo, F.G. and de Pedro, M.A. (1991) Penicillin-Binding Protein 2 is essential for the integrity of growing cells of Escherichia coli pon Bstrains. J. Bacteriol. 173, 4530–4532.Google Scholar
- Ishino, F., Mitsui, K., Tanaki, S. and Matsuhashi, M. (1980) Dual enzyme activities of cell wall peptidoglycan synthesis, peptidoglycan transglycosylase and penicillin sensitive transpeptidase, in purified preparations of Escherichia coli penicillin-binding protein 1A. Biochem. Biophys. Res. Comm. 97, 287–293.PubMedCrossRefGoogle Scholar
- Ishino, F., Park, W., Tomioka, S., Tamaki, S., Takase, I., Kunugita, K., Matsuzawa, H., Asoh, S., Ohta, T., Spratt, B.G. and Matsuhashi, M. (1986) Peptidoglycan synthetic activities in membranes of Escherichia coli caused by overproduction of penicillin-binding protein 2 and RodA protein. J. Biol. Chem. 261,7024–7031.PubMedGoogle Scholar
- Izaki, K., Matsuhashi, M. and Strominger, J.L. (1968) Biosynthesis of the bacterial cell walls. XIII. Peptidoglycan transpeptidase and D-alanine carboxypeptidase: penicillin-sensitive enzymatic reaction in strains of Escherichia coli. J. Biol. Chem. 243, 3180–3192.Google Scholar
- Lleo, M.M., Canepari, P. and Satta, G. (1990) Bacterial cell shape regulation: testing of additional predictions unique to the two-competing-sites model for peptidoglycan assembly and isolation of conditional rodshaped mutants from some wild-type cocci. J. Bacteriol. 172, 3758–3771.PubMedGoogle Scholar
- Vinella, D., D’Ari, R. and Bouloc, P. (1992) Penicillin-binding protein 2 is dispensable in Escherichia coli when ppGpp synthesis is induced. EMBO 11, in press.Google Scholar
- Wachi, M., Doi, M., Tamaki, S., Park, W., Nakajima-Iijima, S. and Matsuhashi, M. (1987) Mutant isolation and molecular cloning oimre genes, which determine cell shape, sensitivity to mecillinam, and amount of penicillin-binding proteins in Escherichia coli. J. Bacteriol. 169,4935–4940.PubMedGoogle Scholar