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

16 Citations (Scopus)

Abstract

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
Volume425
Issue number12
DOIs
Publication statusPublished - 26 Jun 2013
Externally publishedYes

Keywords

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

Cite this

Aylett, Christopher H. S. ; Izore, Thierry ; Amos, Linda A. ; Lowe, Jan. / Structure of the Tubulin/FtsZ-like protein TubZ from Pseudomonas bacteriophage ΦkZ. In: Journal of Molecular Biology. 2013 ; Vol. 425, No. 12. pp. 2164-2173.
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abstract = "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.",
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Structure of the Tubulin/FtsZ-like protein TubZ from Pseudomonas bacteriophage ΦkZ. / Aylett, Christopher H. S.; Izore, Thierry; Amos, Linda A.; Lowe, Jan.

In: Journal of Molecular Biology, Vol. 425, No. 12, 26.06.2013, p. 2164-2173.

Research output: Contribution to journalArticleResearchpeer-review

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