Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12.
The varied effects of beta-lactam antibiotics on cell division, cell elongation, and cell shape in E. coli are shown to be due to the presence of three essential penicillin binding proteins with distinct roles in these three processes. (A) Cell shape: beta-Lactams that specifically result in the production of ovoid cells bind to penicillin binding protein 2 (molecular weight 66,000). A mutant has been isolated that fails to bind beta-lactams to protein 2, and that grows as round cells. (B) Cell division: beta-Lactams that specifically inhibit cell division bind preferentially to penicillin binding protein 3 (molecular weight 60,000). A temperature-sensitive cell division mutant has been shown to have a thermolabile protein 3. (C) Cell elongation: One beta-lactam that preferentially inhibits cell elongation and causes cell lysis binds preferentially to binding protein 1 (molecular weight 91,000). Evidence is presented that penicillin bulge formation is due to the inhibition of proteins 2 and 3 in the absence of inhibition of protein 1.
D000667:Ampicillin / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism*; D001665:Binding Sites; D002455:Cell Division / Q000187:drug effects; D002509:Cephaloridine / Q000378:metabolism; D004926:Escherichia coli / Q000502:physiology*; D007700:Kinetics; D010400:Penicillin G / Q000378:metabolism; D010406:Penicillins / Q000378:metabolism* / Q000494:pharmacology; D011485:Protein Binding; D011955:Receptors, Drug
D001426:Bacterial Proteins; D010406:Penicillins; D011955:Receptors, Drug; D000667:Ampicillin; D002509:Cephaloridine; D010400:Penicillin G