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Arabidopsis plant natriuretic peptide is a novel interactor of rubisco activase

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journal contribution
posted on 16.03.2021, 04:58 by Ilona Turek, C Gehring, Helen Irving
© 2020 by the authors. Licensee MDPI, Basel, Switzerland. Plant 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.

Funding

This 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.

History

Publication Date

01/01/2021

Journal

Life

Volume

11

Issue

1

Article Number

ARTN 21

Pagination

(p. 1-13)

Publisher

MDPI

ISSN

2075-1729

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