Assembly dynamics of the bacterial cell division protein FTSZ: poised at the edge of stability.
FtsZ is a prokaryotic tubulin homolog that assembles into a ring at the future site of cell division. The resulting "Z ring" forms the framework for the division apparatus, and its assembly is regulated throughout the bacterial cell cycle. A highly dynamic structure, the Z ring exhibits continual subunit turnover and the ability to rapidly assemble, disassemble, and, under certain circumstances, relocalize. These in vivo properties are ultimately due to FtsZ's capacity for guanosine triphosphate (GTP)-dependent, reversible polymerization. FtsZ polymer stability appears to be fine-tuned such that subtle changes in its assembly kinetics result in large changes in the Z ring structure. Thus, regulatory proteins that modulate FtsZ's assembly dynamics can cause the ring to rapidly remodel in response to developmental and environmental cues.
Romberg
Laura
L
Institute for Cellular and Chemical Biology, Harvard Medical School, SGM 604, 250 Longwood Avenue, Boston, Massachusetts 02115, USA. laura_romberg@hms.harvard.edu
Levin
Petra Anne
PA
D001412:Bacillus subtilis / Q000378:metabolism / Q000502:physiology; D018797:Cell Cycle Proteins / Q000737:chemistry / Q000378:metabolism*; D002455:Cell Division / Q000502:physiology; D004926:Escherichia coli / Q000378:metabolism / Q000502:physiology; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism*; D019204:GTP-Binding Proteins / Q000737:chemistry / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism; D011487:Protein Conformation
D018797:Cell Cycle Proteins; D029968:Escherichia coli Proteins; C076835:FtsZ84 protein, E coli; D006160:Guanosine Triphosphate; D019204:GTP-Binding Proteins