Structure of the Tubulin/FtsZ-like protein TubZ from Pseudomonas bacteriophage ΦkZ

Christopher H. S. Aylett, Thierry Izore, Linda A. Amos, Jan Lowe

Research output: Contribution to journalArticleResearchpeer-review

20 Citations (Scopus)


Pseudomonas ΦKZ-like bacteriophages encode a group of related tubulin/FtsZ-like proteins believed to be essential for the correct centring of replicated bacteriophage virions within the bacterial host. In this study, we present crystal structures of the tubulin/FtsZ-like protein TubZ from Pseudomonas bacteriophage ΦKZ in both the monomeric and protofilament states, revealing that ΦKZ TubZ undergoes structural changes required to polymerise, forming a canonical tubulin/FtsZ-like protofilament. Combining our structures with previous work, we propose a polymerisation–depolymerisation cycle for the Pseudomonas bacteriophage subgroup of tubulin/FtsZ-like proteins. Electron cryo-microscopy of ΦKZ TubZ filaments polymerised in vitro implies a long-pitch helical arrangement for the constituent protofilaments. Intriguingly, this feature is shared by the other known subgroup of bacteriophage tubulin/FtsZ-like proteins from Clostridium species, which are thought to be involved in partitioning the genomes of bacteriophages adopting a pseudo-lysogenic life cycle.
Original languageEnglish
Pages (from-to)2164-2173
Number of pages10
JournalJournal of Molecular Biology
Issue number12
Publication statusPublished - 26 Jun 2013
Externally publishedYes


  • cytomotive
  • cytoskeletal
  • electron cryo-microscopy
  • filamentous protein
  • X-ray crystallography

Cite this