Tetramerization of ZapA is required for FtsZ bundling

Raúl Pacheco-Gómez, Xi Cheng, Matthew R. Hicks, Corinne J I Smith, David I. Roper, Stephen Addinall, Alison Rodger, Timothy R. Dafforn*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

32 Citations (Scopus)


Prokaryotic cell division is a highly orchestrated process requiring the formation of a wide range of biomolecular complexes, perhaps the most important of these involving the prokaryotic tubulin homologue FtsZ, a fibre-forming GTPase. FtsZ assembles into a ring (the Z-ring) on the inner surface of the inner membrane at the site of cell division. The Z-ring then acts as a recruitment site for at least ten other proteins which form the division apparatus. One of these proteins, ZapA, acts to enhance lateral associations between FtsZ fibres to form bundles. Previously we have expressed, purified and crystallized ZapA and demonstrated that it exists as a tetramer. We also showed that ZapA binds to FtsZ polymers, strongly promoting their bundling, while inhibiting FtsZ GTPase activity by inducing conformational changes in the bound nucleotide. In the present study we investigate the importance of the tetramerization of ZapA on its function. We generated a number of mutant forms of ZapA with the aim of disrupting the dimer - dimer interface. We show that one of these mutants, I83E, is fully folded and binds to FtsZ, but is a constitutive dimer. Using this mutant we show that tetramerization is a requirement for both FtsZ bundling and GTPase modulation activities.

Original languageEnglish
Pages (from-to)795-802
Number of pages8
JournalBiochemical Journal
Issue number3
Publication statusPublished - 1 Feb 2013
Externally publishedYes


  • Cytokinesis
  • Fibre bundling
  • FtsZ
  • Linear dichroism
  • Tetramerization
  • YgfE/ZapA


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