• Title of article

    Structure of the Tubulin/FtsZ-Like Protein TubZ from Pseudomonas Bacteriophage ΦKZ

  • Author/Authors

    Christopher H.S. Aylett، نويسنده , , Thierry Izoré، نويسنده , , Linda A. Amos، نويسنده , , Jan L?we، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2013
  • Pages
    10
  • From page
    2164
  • To page
    2173
  • 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.
  • Keywords
    electron cryo-microscopy , X-ray crystallography , cytoskeletal , cytomotive , filamentous protein
  • Journal title
    Journal of Molecular Biology
  • Serial Year
    2013
  • Journal title
    Journal of Molecular Biology
  • Record number

    1255378