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
Link To Document :
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