The arabidopsis cyclic nucleotide interactome

Handle URI:
http://hdl.handle.net/10754/609438
Title:
The arabidopsis cyclic nucleotide interactome
Authors:
Donaldson, Lara Elizabeth; Meier, Stuart Kurt; Gehring, Christoph A. ( 0000-0003-4355-4591 )
Abstract:
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 nucleotide-dependent 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.
KAUST Department:
Biological and Environmental Sciences and Engineering (BESE) Division
Citation:
The arabidopsis cyclic nucleotide interactome 2016, 14 (1) Cell Communication and Signaling
Publisher:
Springer Science + Business Media
Journal:
Cell Communication and Signaling
Issue Date:
11-May-2016
DOI:
10.1186/s12964-016-0133-2
Type:
Article
ISSN:
1478-811X
Sponsors:
This research was funded by King Abdullah University of Science and Technology.
Is Supplemented By:
Donaldson, L., Meier, S., & Gehring, C. (2016). The arabidopsis cyclic nucleotide interactome. Figshare. https://doi.org/10.6084/m9.figshare.c.3621143; DOI:10.6084/m9.figshare.c.3621143; HANDLE:http://hdl.handle.net/10754/624135
Additional Links:
http://biosignaling.biomedcentral.com/articles/10.1186/s12964-016-0133-2
Appears in Collections:
Articles; Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorDonaldson, Lara Elizabethen
dc.contributor.authorMeier, Stuart Kurten
dc.contributor.authorGehring, Christoph A.en
dc.date.accessioned2016-05-15T13:30:16Zen
dc.date.available2016-05-15T13:30:16Zen
dc.date.issued2016-05-11en
dc.identifier.citationThe arabidopsis cyclic nucleotide interactome 2016, 14 (1) Cell Communication and Signalingen
dc.identifier.issn1478-811Xen
dc.identifier.doi10.1186/s12964-016-0133-2en
dc.identifier.urihttp://hdl.handle.net/10754/609438en
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 nucleotide-dependent 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
dc.description.sponsorshipThis research was funded by King Abdullah University of Science and Technology.en
dc.language.isoenen
dc.publisherSpringer Science + Business Mediaen
dc.relation.urlhttp://biosignaling.biomedcentral.com/articles/10.1186/s12964-016-0133-2en
dc.rightsThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://​creativecommons.​org/​licenses/​by/​4.​0/​), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://​creativecommons.​org/​publicdomain/​zero/​1.​0/​) applies to the data made available in this article, unless otherwise stated.en
dc.subjectcAMPen
dc.subjectcGMPen
dc.subjectCross-talken
dc.subjectCyclic nucleotideen
dc.subjectDefence responseen
dc.subjectH2O2en
dc.subjectHypersensitive responseen
dc.subjectNitric oxideen
dc.subjectReactive oxygen speciesen
dc.subjectSecond messengeren
dc.titleThe arabidopsis cyclic nucleotide interactomeen
dc.typeArticleen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.identifier.journalCell Communication and Signalingen
dc.eprint.versionPublisher's Version/PDFen
dc.contributor.institutionDepartment of Molecular and Cell Biology, University of Cape Town, Private Bag×3, Rondebosch 7701, South Africaen
dc.contributor.affiliationKing Abdullah University of Science and Technology (KAUST)en
kaust.authorDonaldson, Lara Elizabethen
kaust.authorMeier, Stuart Kurten
kaust.authorGehring, Christoph A.en
dc.relation.isSupplementedByDonaldson, L., Meier, S., & Gehring, C. (2016). The arabidopsis cyclic nucleotide interactome. Figshare. https://doi.org/10.6084/m9.figshare.c.3621143en
dc.relation.isSupplementedByDOI:10.6084/m9.figshare.c.3621143en
dc.relation.isSupplementedByHANDLE:http://hdl.handle.net/10754/624135en
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