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A natriuretic peptide from Arabidopsis thaliana (AtPNP-A) can modulate catalase 2 activity

journal contribution
posted on 2020-12-10, 21:02 authored by Ilona TurekIlona Turek, Janet WheelerJanet Wheeler, S Bartels, J Szczurek, Yu Hua Wang, Phil Taylor, C Gehring, Helen IrvingHelen Irving
© 2020, The Author(s). Analogues of vertebrate natriuretic peptides (NPs) present in plants, termed plant natriuretic peptides (PNPs), comprise a novel class of hormones that systemically affect salt and water balance and responses to plant pathogens. Several lines of evidence indicate that Arabidopsis thaliana PNP (AtPNP-A) affects cellular redox homeostasis, which is also typical for the signaling of its vertebrate analogues, but the molecular mechanism(s) of this effect remains elusive. Here we report identification of catalase 2 (CAT2), an antioxidant enzyme, as an interactor of AtPNP-A. The full-length AtPNP-A recombinant protein and the biologically active fragment of AtPNP-A bind specifically to CAT2 in surface plasmon resonance (SPR) analyses, while a biologically inactive scrambled peptide does not. In vivo bimolecular fluorescence complementation (BiFC) showed that CAT2 interacts with AtPNP-A in chloroplasts. Furthermore, CAT2 activity is lower in homozygous atpnp-a knockdown compared with wild type plants, and atpnp-a knockdown plants phenocopy CAT2-deficient plants in their sensitivity to elevated H2O2, which is consistent with a direct modulatory effect of the PNP on the activity of CAT2 and hence H2O2 homeostasis. Our work underlines the critical role of AtPNP-A in modulating the activity of CAT2 and highlights a mechanism of fine-tuning plant responses to adverse conditions by PNPs.


Funding was provided 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. Part of this work was supported by the Australian Research Council [Discovery Project funding scheme (DP0557561, DP0878194)], Australian Postgraduate Award to YHW, and also by La Trobe University. We thank the Salk Institute Genomic Analysis Laboratory for providing the sequence-indexed Arabidopsis T-DNA insertion mutants and Dr Peter Lock (La Trobe University LIMS BioImaging Facility) for assistance with imaging.



  • School of Molecular Sciences

Publication Date



Scientific Reports





Article Number



14p. (p. 1-14)


Springer Nature



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