Journal
ANTIMICROBIAL THERAPEUTICS REVIEWS: THE BACTERIAL CELL WALL AS AN ANTIMICROBIAL TARGET
Volume 1277, Issue -, Pages 8-28Publisher
BLACKWELL SCIENCE PUBL
DOI: 10.1111/j.1749-6632.2012.06818.x
Keywords
cell division; divisome; peptidoglycan; penicillin-binding protein; peptidoglycan hydrolyase; outer membrane; Tol-Pal
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Funding
- Biotechnology and Biological Sciences Research Council [BB/I020012/1] Funding Source: Medline
- BBSRC [BB/I020012/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/I020012/1] Funding Source: researchfish
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Bacterial cell division is facilitated by the divisome, a dynamic multiprotein assembly localizing at mid-cell to synthesize the stress-bearing peptidoglycan and to constrict all cell envelope layers. Divisome assembly occurs in two steps and involves multiple interactions between more than 20 essential and accessory cell division proteins. Well before constriction and while the cell is still elongating, the tubulin-like FtsZ and early cell division proteins form a ring-like structure at mid-cell. Cell division starts once certain peptidoglycan enzymes and their activators have moved to the FtsZ-ring. Gram-negative bacteria like Escherichia coli simultaneously synthesize and cleave the septum peptidoglycan during division leading to a constriction. The outer membrane constricts together with the peptidoglycan layer with the help of the transenvelope spanning Tol-Pal system.
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