The order of the ring: assembly of Escherichia coli cell division components.
Topological cues appear to override temporal events in the assembly of the Escherichia coli cell division ring. When a procedure that allows the recruitment of ring components based on their topological properties is used, a concerted mode of assembly of several components of the divisome, rather than a strict linear mode, is revealed. Three multimolecular complexes, the proto-ring, the periplasmic connector and the peptidoglycan factory, show some degree of concertation for their assembly. In addition, back-recruitment of all late proteins except FtsN into the division ring occurs even in the absence of proteins incorporated at earlier stages, i.e. FtsA or FtsQ.
Vicente
Miguel
M
Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas, Campus de Cantoblanco, c/Darwin 3, 28049 Madrid, Spain. mvicente@cnb.uam.es
Rico
Ana Isabel
AI
D018797:Cell Cycle Proteins / Q000378:metabolism* / Q000502:physiology; D002455:Cell Division / Q000502:physiology; D004926:Escherichia coli / Q000166:cytology / Q000378:metabolism* / Q000502:physiology; D029968:Escherichia coli Proteins / Q000378:metabolism* / Q000502:physiology; D008565:Membrane Proteins / Q000378:metabolism / Q000494:pharmacology; D008954:Models, Biological; D046912:Multiprotein Complexes / Q000378:metabolism / Q000502:physiology; D010457:Peptidoglycan / Q000378:metabolism
D018797:Cell Cycle Proteins; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D046912:Multiprotein Complexes; D010457:Peptidoglycan