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FEBS Lett. 2001 Apr 6;494(1-2):34-7.

Substitution of a conserved aspartate allows cation-induced polymerization of FtsZ.

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Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan, The Netherlands.


The prokaryotic tubulin homologue FtsZ polymerizes in vitro in a nucleotide dependent fashion. Here we report that replacement of the strictly conserved Asp212 residue of Escherichia coli FtsZ by a Cys or Asn, but not by a Glu residue results in FtsZ that polymerizes with divalent cations in the absence of added GTP. FtsZ D212C and D212N mutants co-purify with GTP as bound nucleotide, providing an explanation for the unusual phenotype. We conclude that D212 plays a critical role in the coordination of a metal ion and the nucleotide at the interface of two FtsZ monomers.

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