Mutations in the bacterial cell division protein FtsZ highlight the role of GTP binding and longitudinal subunit interactions in assembly and function

@article{Arjes2015MutationsIT,
  title={Mutations in the bacterial cell division protein FtsZ highlight the role of GTP binding and longitudinal subunit interactions in assembly and function},
  author={Heidi A. Arjes and Bradley Lai and Ezinwanne Rosemary Emelue and Adriana Steinbach and Petra Anne Levin},
  journal={BMC Microbiology},
  year={2015},
  volume={15}
}
  • Heidi A. Arjes, Bradley Lai, +2 authors Petra Anne Levin
  • Published 2015
  • Biology, Medicine
  • BMC Microbiology
  • BackgroundAssembly of the tubulin-like GTPase, FtsZ, at the future division site initiates the process of bacterial cytokinesis. The FtsZ ring serves as a platform for assembly of the division machinery and constricts at the leading edge of the invaginating septum during cytokinesis. In vitro, FtsZ assembles in a GTP-dependent manner, forming straight filaments that curve upon GTP hydrolysis. FtsZ binds but cannot hydrolyze GTP as a monomer. Instead, the active site for GTP hydrolysis is formed… CONTINUE READING

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    Guanine nucleotide-dependent assembly of FtsZ into filaments.

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