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

• Published in: FEBS letters Vol. 494; no. 1; pp. 34 - 37
• Main Authors: Scheffers, Dirk-Jan, de Wit, Janny G, den Blaauwen, Tanneke, Driessen, Arnold J.M
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 06-04-2001
• Subjects: Amino Acid Substitution; Aspartic Acid - genetics; Aspartic Acid - metabolism; Aspartic Acid - physiology; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Cation; Cations, Divalent; Cell division; Cytoskeletal Proteins; DTT, 1,4-dithio-DL-threitol; FtsZ; Guanosine Triphosphate - metabolism; MTSEA, methanethiosulfonate-ethylammonium; MTSES, methanethiosulfonate-ethylsulfonate; Mutagenesis, Site-Directed; NEM, N-ethylmaleimide; Polymerization; Polymers; Tubulin; NEM, N-ethylmaleimide; Tubulin; Cation; FtsZ; Polymerization; Cell division; MTSES, methanethiosulfonate-ethylsulfonate; DTT, 1,4-dithio- DL-threitol; MTSEA, methanethiosulfonate-ethylammonium
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(01)02310-9

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.