The arabidopsis cyclic nucleotide interactome

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dc.contributor.authorDonaldson, Lara
dc.contributor.authorMeier, Stuart
dc.contributor.authorGehring, Christoph
dc.date.accessioned2016-05-19T13:52:35Z
dc.date.available2016-05-19T13:52:35Z
dc.date.issued2016-05-11
dc.date.updated2016-05-19T09:34:11Z
dc.description.abstractBackground: Cyclic nucleotides have been shown to play important signaling roles in many physiological processes in plants including photosynthesis and defence. Despite this, little is known about cyclic nucleotidedependent signaling mechanisms in plants since the downstream target proteins remain unknown. This is largely due to the fact that bioinformatics searches fail to identify plant homologs of protein kinases and phosphodiesterases that are the main targets of cyclic nucleotides in animals. Methods: An affinity purification technique was used to identify cyclic nucleotide binding proteins in Arabidopsis thaliana. The identified proteins were subjected to a computational analysis that included a sequence, transcriptional co-expression and functional annotation analysis in order to assess their potential role in plant cyclic nucleotide signaling. Results: A total of twelve cyclic nucleotide binding proteins were identified experimentally including key enzymes in the Calvin cycle and photorespiration pathway. Importantly, eight of the twelve proteins were shown to contain putative cyclic nucleotide binding domains. Moreover, the identified proteins are post-translationally modified by nitric oxide, transcriptionally co-expressed and annotated to function in hydrogen peroxide signaling and the defence response. The activity of one of these proteins, GLYGOLATE OXIDASE 1, a photorespiratory enzyme that produces hydrogen peroxide in response to Pseudomonas, was shown to be repressed by a combination of cGMP and nitric oxide treatment. Conclusions: We propose that the identified proteins function together as points of cross-talk between cyclic nucleotide, nitric oxide and reactive oxygen species signaling during the defence response.en_ZA
dc.identifier.apacitationDonaldson, L., Meier, S., & Gehring, C. (2016). The arabidopsis cyclic nucleotide interactome. <i>Cell Communication and Signaling</i>, http://hdl.handle.net/11427/19728en_ZA
dc.identifier.chicagocitationDonaldson, Lara, Stuart Meier, and Christoph Gehring "The arabidopsis cyclic nucleotide interactome." <i>Cell Communication and Signaling</i> (2016) http://hdl.handle.net/11427/19728en_ZA
dc.identifier.citationDonaldson, L., Meier, S., & Gehring, C. (2016). The arabidopsis cyclic nucleotide interactome. Cell Communication and Signaling, 14(1), 1.en_ZA
dc.identifier.issn1478-811Xen_ZA
dc.identifier.ris TY - Journal Article AU - Donaldson, Lara AU - Meier, Stuart AU - Gehring, Christoph AB - Background: Cyclic nucleotides have been shown to play important signaling roles in many physiological processes in plants including photosynthesis and defence. Despite this, little is known about cyclic nucleotidedependent signaling mechanisms in plants since the downstream target proteins remain unknown. This is largely due to the fact that bioinformatics searches fail to identify plant homologs of protein kinases and phosphodiesterases that are the main targets of cyclic nucleotides in animals. Methods: An affinity purification technique was used to identify cyclic nucleotide binding proteins in Arabidopsis thaliana. The identified proteins were subjected to a computational analysis that included a sequence, transcriptional co-expression and functional annotation analysis in order to assess their potential role in plant cyclic nucleotide signaling. Results: A total of twelve cyclic nucleotide binding proteins were identified experimentally including key enzymes in the Calvin cycle and photorespiration pathway. Importantly, eight of the twelve proteins were shown to contain putative cyclic nucleotide binding domains. Moreover, the identified proteins are post-translationally modified by nitric oxide, transcriptionally co-expressed and annotated to function in hydrogen peroxide signaling and the defence response. The activity of one of these proteins, GLYGOLATE OXIDASE 1, a photorespiratory enzyme that produces hydrogen peroxide in response to Pseudomonas, was shown to be repressed by a combination of cGMP and nitric oxide treatment. Conclusions: We propose that the identified proteins function together as points of cross-talk between cyclic nucleotide, nitric oxide and reactive oxygen species signaling during the defence response. DA - 2016-05-11 DB - OpenUCT DO - 10.1186/s12964-016-0133-2 DP - University of Cape Town J1 - Cell Communication and Signaling KW - cAMP KW - cGMP KW - Cross-talk KW - Cyclic nucleotide KW - Defence response KW - Hypersensitive response KW - Nitric oxide KW - Reactive oxygen species KW - Second messenger LK - https://open.uct.ac.za PB - University of Cape Town PY - 2016 SM - 1478-811X T1 - The arabidopsis cyclic nucleotide interactome TI - The arabidopsis cyclic nucleotide interactome UR - http://hdl.handle.net/11427/19728 ER - en_ZA
dc.identifier.urihttp://dx.doi.org/10.1186/s12964-016-0133-2
dc.identifier.urihttp://hdl.handle.net/11427/19728
dc.identifier.vancouvercitationDonaldson L, Meier S, Gehring C. The arabidopsis cyclic nucleotide interactome. Cell Communication and Signaling. 2016; http://hdl.handle.net/11427/19728.en_ZA
dc.languageengen_ZA
dc.language.rfc3066en
dc.publisherBioMed Centralen_ZA
dc.publisher.departmentDepartment of Molecular and Cell Biologyen_ZA
dc.publisher.facultyFaculty of Scienceen_ZA
dc.publisher.institutionUniversity of Cape Town
dc.rightsCreative Commons Attribution 4.0 International (CC BY 4.0)*
dc.rights.holderDonaldson et al.
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en_ZA
dc.sourceCell Communication and Signalingen_ZA
dc.source.urihttp://www.biosignaling.com/
dc.subjectcAMP
dc.subjectcGMP
dc.subjectCross-talk
dc.subjectCyclic nucleotide
dc.subjectDefence response
dc.subjectHypersensitive response
dc.subjectNitric oxide
dc.subjectReactive oxygen species
dc.subjectSecond messenger
dc.titleThe arabidopsis cyclic nucleotide interactomeen_ZA
dc.typeJournal Articleen_ZA
uct.type.filetypeText
uct.type.filetypeImage
uct.type.publicationResearchen_ZA
uct.type.resourceArticleen_ZA
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