Substitution of a conserved aspartate allows cation-induced polymerization of FtsZ.
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.
Scheffers
D J
DJ
Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan, The Netherlands.
de Wit
J G
JG
den Blaauwen
T
T
Driessen
A J
AJ
D019943:Amino Acid Substitution; D001224:Aspartic Acid / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D002413:Cations, Divalent; D003598:Cytoskeletal Proteins; D006160:Guanosine Triphosphate / Q000378:metabolism; D016297:Mutagenesis, Site-Directed; D011108:Polymers
D001426:Bacterial Proteins; D002413:Cations, Divalent; D003598:Cytoskeletal Proteins; C071525:FtsZ protein, Bacteria; D011108:Polymers; D001224:Aspartic Acid; D006160:Guanosine Triphosphate