University Of Tasmania
148963 - Salinity effects on guard cell proteome in Chenopodium quinoa.pdf (3.25 MB)
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Salinity effects on guard cell proteome in Chenopodium quinoa

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journal contribution
posted on 2023-05-21, 05:58 authored by Rasouli, F, Ali Kiani-Pouya, Svetlana ShabalaSvetlana Shabala, Li, L, Tahir, A, Yu, M, Hedrich, R, Chen, Z, Richard WilsonRichard Wilson, Zhang, H, Sergey ShabalaSergey Shabala

Epidermal fragments enriched in guard cells (GCs) were isolated from the halophyte quinoa (Chenopodium quinoa Wild.) species, and the response at the proteome level was studied after salinity treatment of 300 mM NaCl for 3 weeks. In total, 2147 proteins were identified, of which 36% were differentially expressed in response to salinity stress in GCs. Up and downregulated proteins included signaling molecules, enzyme modulators, transcription factors and oxidoreductases. The most abundant proteins induced by salt treatment were desiccation-responsive protein 29B (50-fold), osmotin-like protein OSML13 (13-fold), polycystin-1, lipoxygenase, alpha-toxin, and triacylglycerol lipase (PLAT) domain-containing protein 3-like (eight-fold), and dehydrin early responsive to dehydration (ERD14) (eight-fold). Ten proteins related to the gene ontology term "response to ABA" were upregulated in quinoa GC; this included aspartic protease, phospholipase D and plastid-lipid-associated protein. Additionally, seven proteins in the sucrose-starch pathway were upregulated in the GC in response to salinity stress, and accumulation of tryptophan synthase and L-methionine synthase (enzymes involved in the amino acid biosynthesis) was observed. Exogenous application of sucrose and tryptophan, L-methionine resulted in reduction in stomatal aperture and conductance, which could be advantageous for plants under salt stress. Eight aspartic proteinase proteins were highly upregulated in GCs of quinoa, and exogenous application of pepstatin A (an inhibitor of aspartic proteinase) was accompanied by higher oxidative stress and extremely low stomatal aperture and conductance, suggesting a possible role of aspartic proteinase in mitigating oxidative stress induced by saline conditions.


Publication title

International Journal of Molecular Sciences



Article number









Tasmanian Institute of Agriculture (TIA)


Molecular Diversity Preservation International

Place of publication

Matthaeusstrasse 11, Basel, Switzerland, Ch-4057

Rights statement

Copyright: © 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons 4.0 International (CC BY 4.0) license (

Repository Status

  • Open

Socio-economic Objectives

Horticultural crops not elsewhere classified; Expanding knowledge in the biological sciences