Tubulin homolog TubZ in a phage-encoded partition system
Partition systems are responsible for the process whereby large and essential plasmids are accurately positioned to daughter cells during bacterial division. They are typically made of three components: a centromere-like DNA zone, an adaptor protein, and an assembling protein that is either a Walker...
| Autores: | , , , |
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| Tipo de recurso: | artículo |
| Fecha de publicación: | 2012 |
| País: | España |
| Institución: | Instituto de Salud Carlos III (ISCIII) |
| Repositorio: | Repisalud |
| Idioma: | inglés |
| OAI Identifier: | oai:repisalud.isciii.es:20.500.12105/17439 |
| Acceso en línea: | http://hdl.handle.net/20.500.12105/17439 |
| Access Level: | acceso abierto |
| Palabra clave: | Models, Molecular Amino Acid Sequence Bacterial Proteins Bacteriophages Base Sequence Biophysics Centromere Cloning, Molecular Clostridium botulinum Cluster Analysis Computational Biology Crystallization Cytokinesis Molecular Sequence Data Multiprotein Complexes Phylogeny Plasmids Sequence Analysis, DNA Tubulin |
| Sumario: | Partition systems are responsible for the process whereby large and essential plasmids are accurately positioned to daughter cells during bacterial division. They are typically made of three components: a centromere-like DNA zone, an adaptor protein, and an assembling protein that is either a Walker-box ATPase (type I) or an actin-like ATPase (type II). A recently described type III segregation system has a tubulin/FtsZ-like protein, called TubZ, for plasmid movement. Here, we present the 2.3 Å structure and dynamic assembly of a TubZ tubulin homolog from a bacteriophage and unravel the Clostridium botulinum phage c-st type III partition system. Using biochemical and biophysical approaches, we prove that a gene upstream from tubZ encodes the partner TubR and localize the centromeric region (tubS), both of which are essential for anchoring phage DNA to the motile TubZ filaments. Finally, we describe a conserved fourth component, TubY, which modulates the TubZ-R-S complex interaction. |
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