Publication:
Tubulin homolog TubZ in a phage-encoded partition system

dc.contributor.authorOliva, María A
dc.contributor.authorMartin-Galiano, Antonio Javier
dc.contributor.authorSakaguchi, Yoshihiko
dc.contributor.authorAndreu, José M
dc.date.accessioned2024-02-02T17:21:15Z
dc.date.available2024-02-02T17:21:15Z
dc.date.issued2012-05-15
dc.description.abstractPartition 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.es_ES
dc.description.peerreviewedes_ES
dc.format.number20es_ES
dc.format.page7711-7716es_ES
dc.format.volume109es_ES
dc.identifier.citationProc Natl Acad Sci USA. 2012 May 15;109(20):7711-6.es_ES
dc.identifier.doi10.1073/pnas.1121546109es_ES
dc.identifier.e-issn1091-6490es_ES
dc.identifier.journalProceedings of the National Academy of Sciences of the United States of Americaes_ES
dc.identifier.otherhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3356609/pdf/pnas.201121546.pdf
dc.identifier.pubmedID22538818es_ES
dc.identifier.urihttp://hdl.handle.net/20.500.12105/17439
dc.language.isoenges_ES
dc.publisherNational Academy of Scienceses_ES
dc.relation.publisherversionhttps://doi.org/10.1073/pnas.1121546109es_ES
dc.repisalud.centroISCIII::Centro Nacional de Microbiologíaes_ES
dc.repisalud.institucionISCIIIes_ES
dc.rights.accessRightsopen accesses_ES
dc.rights.licenseAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectDNA segregationes_ES
dc.subjectCytomotive filamentses_ES
dc.subjectVirulencees_ES
dc.subjectPlasmid partitioninges_ES
dc.subject.meshModels, Moleculares_ES
dc.subject.meshAmino Acid Sequencees_ES
dc.subject.meshBacterial Proteinses_ES
dc.subject.meshBacteriophageses_ES
dc.subject.meshBase Sequencees_ES
dc.subject.meshBiophysicses_ES
dc.subject.meshCentromerees_ES
dc.subject.meshCloning, Moleculares_ES
dc.subject.meshClostridium botulinumes_ES
dc.subject.meshCluster Analysises_ES
dc.subject.meshComputational Biologyes_ES
dc.subject.meshCrystallizationes_ES
dc.subject.meshCytokinesises_ES
dc.subject.meshMolecular Sequence Dataes_ES
dc.subject.meshMultiprotein Complexeses_ES
dc.subject.meshPhylogenyes_ES
dc.subject.meshPlasmidses_ES
dc.subject.meshSequence Analysis, DNAes_ES
dc.subject.meshTubulines_ES
dc.titleTubulin homolog TubZ in a phage-encoded partition systemes_ES
dc.typeresearch articlees_ES
dc.type.hasVersionVoRes_ES
dspace.entity.typePublication
relation.isAuthorOfPublicationa05be95c-83ed-4217-ab14-cbca92cd5279
relation.isAuthorOfPublication.latestForDiscoverya05be95c-83ed-4217-ab14-cbca92cd5279

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