Phosphorylation of serine residue modulates cotton Di19-1 and Di19-2 activities for responding to high salinity stress and abscisic acid signaling
| Autor: | Rong Hu, Xue-Bao Li, Li-Xia Qin, Gang Li, Xiao-Ying Nie, Wen-Liang Xu |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0106 biological sciences
0301 basic medicine Salinity Mutant Arabidopsis Germination Biology 01 natural sciences Article Serine 03 medical and health sciences chemistry.chemical_compound Gene Expression Regulation Plant Stress Physiological Amino Acid Sequence Phosphorylation Protein kinase A Abscisic acid Plant Proteins Gossypium Multidisciplinary Calcium-Binding Proteins food and beverages biology.organism_classification Molecular biology Droughts Transport protein Protein Transport Phenotype 030104 developmental biology chemistry Seedlings Mutation Calcium Signal transduction Protein Kinases Abscisic Acid Signal Transduction 010606 plant biology & botany |
| Zdroj: | Scientific Reports |
| ISSN: | 2045-2322 |
| DOI: | 10.1038/srep20371 |
| Popis: | Di19 (drought-induced protein 19) family is a novel type of Cys2/His2 zinc-finger proteins. In this study, we demonstrated that cotton Di19-1 and Di19-2 (GhDi19-1/-2) proteins could be phosphorylated in vitro by the calcium-dependent protein kinase (CDPK). Mutation of Ser to Ala in N-terminus of GhDi19-1/-2 led to the altered subcellular localization of the two proteins, but the constitutively activated form (Ser was mutated to Asp) of GhDi19-1/-2 still showed the nuclear localization. GhDi19-1/-2 overexpression transgenic Arabidopsis seedlings displayed the hypersensitivity to high salinity and abscisic acid (ABA). However, Ser site-mutated GhDi19-1(S116A) and GhDi19-2(S114A) and Ser and Thr double sites-mutated GhDi19-1(S/T-A/A) and GhDi19-2(S/T-A/A) transgenic Arabidopsis did not show the salt- and ABA-hypersensitive phenotypes. In contrast, overexpression of Thr site-mutated GhDi19-1(T114A) and GhDi19-2(T112A) in Arabidopsis still resulted in salt- and ABA-hypersensitivity phenotypes, like GhDi19-1/-2 transgenic lines. Overexpression of GhDi19-1/-2 and their constitutively activated forms in Atcpk11 background could recover the salt- and ABA-insensitive phenotype of the mutant. Thus, our results demonstrated that Ser phosphorylation (not Thr phosphorylation) is crucial for functionally activating GhDi19-1/-2 in response to salt stress and ABA signaling during early plant development and GhDi19-1/-2 proteins may be downstream targets of CDPKs in ABA signal pathway. |
| Databáze: | OpenAIRE |
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