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dc.contributor.authorTurek, Ilona
dc.contributor.authorGehring, Christoph A
dc.contributor.authorIrving, H R
dc.date.accessioned2021-01-05T11:48:17Z
dc.date.available2021-01-05T11:48:17Z
dc.date.issued2020-12-31
dc.date.submitted2020-11-30
dc.identifier.citationTurek, I., Gehring, C., & Irving, H. (2020). Arabidopsis Plant Natriuretic Peptide Is a Novel Interactor of Rubisco Activase. Life, 11(1), 21. doi:10.3390/life11010021
dc.identifier.issn2075-1729
dc.identifier.doi10.3390/life11010021
dc.identifier.urihttp://hdl.handle.net/10754/666819
dc.description.abstractPlant natriuretic peptides (PNPs) are a group of systemically acting peptidic hormones affecting solute and solvent homeostasis and responses to biotrophic pathogens. Although an increasing body of evidence suggests PNPs modulate plant responses to biotic and abiotic stress, which could lead to their potential biotechnological application by conferring increased stress tolerance to plants, the exact mode of PNPs action is still elusive. In order to gain insight into PNP-dependent signalling, we set out to identify interactors of PNP present in the model plant Arabidopsis thaliana, termed AtPNP-A. Here, we report identification of rubisco activase (RCA), a central regulator of photosynthesis converting Rubisco catalytic sites from a closed to an open conformation, as an interactor of AtPNP-A through affinity isolation followed by mass spectrometric identification. Surface plasmon resonance (SPR) analyses reveals that the full-length recombinant AtPNP-A and the biologically active fragment of AtPNP-A bind specifically to RCA, whereas a biologically inactive scrambled peptide fails to bind. These results are considered in the light of known functions of PNPs, PNP-like proteins, and RCA in biotic and abiotic stress responses.
dc.description.sponsorshipWe thank KAUST Bioscience Core Laboratory for assistance with mass spectrometric analyses.
dc.description.sponsorshipThis research was supported by Division of Biological and Environmental Sciences and Engineering, King Abdullah University of Science and Technology. Ilona Turek was supported by a King Abdullah University of Science and Technology doctoral scholarship.
dc.publisherMDPI AG
dc.relation.urlhttps://www.mdpi.com/2075-1729/11/1/21
dc.rightsThis article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license.
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.titleArabidopsis Plant Natriuretic Peptide Is a Novel Interactor of Rubisco Activase
dc.typeArticle
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.contributor.departmentBioscience Program
dc.contributor.departmentChemical Engineering Program
dc.contributor.departmentMolecular Signalling Group
dc.contributor.departmentPhysical Science and Engineering (PSE) Division
dc.identifier.journalLife
dc.eprint.versionPublisher's Version/PDF
dc.contributor.institutionDepartment of Pharmacy and Biomedical Sciences, La Trobe Institute for Molecular Science, La Trobe University, Bendigo, VIC 3552, Australia.
dc.contributor.institutionDepartment of Chemistry, Biology and Biotechnology, University of Perugia, 06121 Perugia, Italy.
dc.identifier.volume11
dc.identifier.issue1
dc.identifier.pages21
kaust.personTurek, Ilona
kaust.personGehring, Christoph A.
dc.date.accepted2020-12-29
refterms.dateFOA2021-01-05T11:49:29Z
kaust.acknowledged.supportUnitKAUST Bioscience Core Laboratory


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This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license.
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