Salinity effects on guard cell proteome in Chenopodium quinoa
Autor: | Ayesha Tahir, Zhong-Hua Chen, Lana Shabala, Sergey Shabala, Rainer Hedrich, Heng Zhang, Min Yu, Fatemeh Rasouli, Ali Kiani-Pouya, Richard Wilson, Leiting Li |
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Jazyk: | angličtina |
Rok vydání: | 2021 |
Předmět: |
0106 biological sciences
0301 basic medicine Salinity Proteome stomata Tryptophan synthase 01 natural sciences Chenopodium quinoa Catalysis Article Inorganic Chemistry lcsh:Chemistry 03 medical and health sciences chemistry.chemical_compound Guard cell Physical and Theoretical Chemistry Molecular Biology lcsh:QH301-705.5 Spectroscopy Amino acid synthesis Plant Proteins salt stress chemistry.chemical_classification biology Phospholipase D Organic Chemistry proteomics analysis Tryptophan quinoa General Medicine Salt Tolerance Computer Science Applications 030104 developmental biology ddc:580 chemistry Biochemistry lcsh:Biology (General) lcsh:QD1-999 biology.protein guard cell Pepstatin 010606 plant biology & botany |
Zdroj: | International Journal of Molecular Sciences Volume 22 Issue 1 International Journal of Molecular Sciences, Vol 22, Iss 428, p 428 (2021) |
DOI: | 10.3390/ijms22010428 |
Popis: | 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 &ldquo response to ABA&rdquo were upregulated in quinoa GC this included aspartic protease, phospholipase D and plastid-lipid-associated protein. Additionally, seven proteins in the sucrose&ndash 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. |
Databáze: | OpenAIRE |
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