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Publication Abstract from PubMed

Pseudomonas PhiKZ-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 PhiKZ in both the monomeric and protofilament states, revealing that PhiKZ 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 PhiKZ 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.

Structure of the Tubulin/FtsZ-Like Protein TubZ from Pseudomonas Bacteriophage PhiKZ.,Aylett CH, Izore T, Amos LA, Lowe J J Mol Biol. 2013 Mar 22. pii: S0022-2836(13)00167-8. doi:, 10.1016/j.jmb.2013.03.019. PMID:23528827^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.