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dc.contributor.authorde Souza, Tiago Anthony
dc.contributor.authorSoprano, Adriana Santos
dc.contributor.authorde Lira, Nayara Patricia Vieira
dc.contributor.authorQuaresma, Alexandre J.C.
dc.contributor.authorPaes Leme, Adriana Franco
dc.contributor.authorBenedetti, Celso Eduardo
dc.date2022-08-11T08:08:03.000
dc.date.accessioned2022-08-23T15:40:34Z
dc.date.available2022-08-23T15:40:34Z
dc.date.issued2012-02-22
dc.date.submitted2013-01-02
dc.identifier.citation<p>de Souza TA, Soprano AS, Lira NPVd, Quaresma AJC, Pauletti BA, et al. (2012) The TAL Effector PthA4 Interacts with Nuclear Factors Involved in RNA-Dependent Processes Including a HMG Protein That Selectively Binds Poly(U) RNA. PLoS ONE 7(2): e32305. doi:10.1371/journal.pone.0032305. <a href="http://dx.doi.org/10.1371/journal.pone.0032305" target="_blank">Link to article on publisher's website</a></p>
dc.identifier.doi10.1371/journal.pone.0032305
dc.identifier.pmid22384209
dc.identifier.urihttp://hdl.handle.net/20.500.14038/26431
dc.description.abstractPlant pathogenic bacteria utilize an array of effector proteins to cause disease. Among them, transcriptional activator-like (TAL) effectors are unusual in the sense that they modulate transcription in the host. Although target genes and DNA specificity of TAL effectors have been elucidated, how TAL proteins control host transcription is poorly understood. Previously, we showed that the Xanthomonas citri TAL effectors, PthAs 2 and 3, preferentially targeted a citrus protein complex associated with transcription control and DNA repair. To extend our knowledge on the mode of action of PthAs, we have identified new protein targets of the PthA4 variant, required to elicit canker on citrus. Here we show that all the PthA4-interacting proteins are DNA and/or RNA-binding factors implicated in chromatin remodeling and repair, gene regulation and mRNA stabilization/modification. The majority of these proteins, including a structural maintenance of chromosomes protein (CsSMC), a translin-associated factor X (CsTRAX), a VirE2-interacting protein (CsVIP2), a high mobility group (CsHMG) and two poly(A)-binding proteins (CsPABP1 and 2), interacted with each other, suggesting that they assemble into a multiprotein complex. CsHMG was shown to bind DNA and to interact with the invariable leucine-rich repeat region of PthAs. Surprisingly, both CsHMG and PthA4 interacted with PABP1 and 2 and showed selective binding to poly(U) RNA, a property that is novel among HMGs and TAL effectors. Given that homologs of CsHMG, CsPABP1, CsPABP2, CsSMC and CsTRAX in other organisms assemble into protein complexes to regulate mRNA stability and translation, we suggest a novel role of TAL effectors in mRNA processing and translational control.
dc.language.isoen_US
dc.publisherPublic Library of Science
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=22384209&dopt=Abstract">Link to article in PubMed</a>
dc.rights<p>Copyright 2012 de Souza et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.</p>
dc.subjectBacterial Proteins
dc.subjectPoly U
dc.subjectRNA
dc.subjectXanthomonas
dc.subjectCell and Developmental Biology
dc.subjectCell Biology
dc.titleThe TAL effector PthA4 interacts with nuclear factors involved in RNA-dependent processes including a HMG protein that selectively binds poly(U) RNA
dc.typeJournal Article
dc.source.journaltitlePLoS ONE
dc.source.volume7
dc.source.issue2
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1110&amp;context=cellbiology_pp&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/cellbiology_pp/111
dc.identifier.contextkey3559550
refterms.dateFOA2022-08-23T15:40:34Z
html.description.abstract<p>Plant pathogenic bacteria utilize an array of effector proteins to cause disease. Among them, transcriptional activator-like (TAL) effectors are unusual in the sense that they modulate transcription in the host. Although target genes and DNA specificity of TAL effectors have been elucidated, how TAL proteins control host transcription is poorly understood. Previously, we showed that the Xanthomonas citri TAL effectors, PthAs 2 and 3, preferentially targeted a citrus protein complex associated with transcription control and DNA repair. To extend our knowledge on the mode of action of PthAs, we have identified new protein targets of the PthA4 variant, required to elicit canker on citrus. Here we show that all the PthA4-interacting proteins are DNA and/or RNA-binding factors implicated in chromatin remodeling and repair, gene regulation and mRNA stabilization/modification. The majority of these proteins, including a structural maintenance of chromosomes protein (CsSMC), a translin-associated factor X (CsTRAX), a VirE2-interacting protein (CsVIP2), a high mobility group (CsHMG) and two poly(A)-binding proteins (CsPABP1 and 2), interacted with each other, suggesting that they assemble into a multiprotein complex. CsHMG was shown to bind DNA and to interact with the invariable leucine-rich repeat region of PthAs. Surprisingly, both CsHMG and PthA4 interacted with PABP1 and 2 and showed selective binding to poly(U) RNA, a property that is novel among HMGs and TAL effectors. Given that homologs of CsHMG, CsPABP1, CsPABP2, CsSMC and CsTRAX in other organisms assemble into protein complexes to regulate mRNA stability and translation, we suggest a novel role of TAL effectors in mRNA processing and translational control.</p>
dc.identifier.submissionpathcellbiology_pp/111
dc.contributor.departmentDepartment of Cell and Developmental Biology
dc.source.pagese32305


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