ArticlePlant molecular biology2005
Salicylic acid-inducible Arabidopsis CK2-like activity phosphorylates TGA2.
Article in Plant molecular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 63 citations in OpenAlex.
- Unveiling the TGA gene family in Qingke (Hordeum vulgare L. var. nudum) and the role of HvnTGA2 in host-pathogen interaction.BMC plant biology · 2026Article
- Salicylic acid accumulation: emerging molecular players and novel perspectives on plant development and nutrition.Journal of experimental botany · 2025Review
- A nuclear tRNA-derived fragment triggers immunity in Arabidopsis.Communications biology · 2025Article
- Arabidopsis MORC1 and MED9 Interact to Regulate Defense Gene Expression and Plant Fitness.The plant pathology journal · 2024Article
- CK2 promotes jasmonic acid signaling response by phosphorylating MYC2 in Arabidopsis.Nucleic acids research · 2023Article
- Phosphorylation of OsTGA5 by casein kinase II compromises its suppression of defense-related gene transcription in rice.The Plant cell · 2022Article
- TGA transcription factors-Structural characteristics as basis for functional variability.Frontiers in plant science · 2022Review
- Effects of Abscisic Acid and Salicylic Acid on Gene Expression in the Antiviral RNA Silencing Pathway in Arabidopsis.International journal of molecular sciences · 2019Article
- TCO, a Putative Transcriptional Regulator inInternational journal of molecular sciences · 2018Article
- TGA2 signaling in response to reactive electrophile species is not dependent on cysteine modification of TGA2.PloS one · 2018Article
- Quantitative Phosphoproteomic Analysis Reveals Shared and Specific Targets ofMolecular & cellular proteomics : MCP · 2018Article
- Article
- Salicylic acid interferes with GFP fluorescence in vivo.Journal of experimental botany · 2017Article
- Phosphorylation Affects DNA-Binding of the Senescence-Regulating bZIP Transcription Factor GBF1.Plants (Basel, Switzerland) · 2015Article
- Emerging roles of protein kinase CK2 in abscisic acid signaling.Frontiers in plant science · 2015Review
- Abscisic acid deficiency antagonizes high-temperature inhibition of disease resistance through enhancing nuclear accumulation of resistance proteins SNC1 and RPS4 in Arabidopsis.The Plant cell · 2012Article
- The p23 co-chaperone protein is a novel substrate of CK2 in Arabidopsis.Molecular and cellular biochemistry · 2011Article
- About the role of CK2 in plant signal transduction.Molecular and cellular biochemistry · 2011Article
- Dual-function transcription factors and their entourage: unique and unifying themes governing two pathogenesis-related genes.Plant signaling & behavior · 2010Review
- Genetic interactions of TGA transcription factors in the regulation of pathogenesis-related genes and disease resistance in Arabidopsis.Plant physiology · 2007Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We demonstrate that TGA2, TGA5 and TGA6, and TGA3 to a lesser extent, are phosphorylated by an activity in rabbit reticulocytes. Using deletion and point mutagenesis of TGA2, three amino acid (aa) residues, (11)Ser, (12)Thr and (16)Thr, were found to be critical for efficient phosphorylation by a kinase(s) in rabbit reticulocytes. These three residues also were important for phosphorylation by recombinant human Casein Kinase II (CK2) and by a CK2-like kinase in Arabidopsis leaf extracts. Salicylic acid (SA) treatment enhanced the phosphorylation of recombinant TGA2 in vitro; it also enhanced phosphorylation of a TGA2-GFP fusion protein in vivo. By contrast, in vivo phosphorylation of a TGA2-A-GFP fusion protein, in which the (11)Ser, (12)Thr and (16)Thr residues were mutated to non-phosphorylable alanine, was only poorly if at all stimulated by SA treatment. Mutation of the putative CK2 phosphorylation motif did not affect nuclear localization of TGA2. However, the DNA binding activity of TGA2 was reduced by CK2 treatment, whereas that of TGA2-A was unaffected; TGA2's DNA binding activity after incubation in a rabbit reticulocyte lysate also was substantially lower than that of comparably treated TGA2-A. Taken together, these results suggest that phosphorylation at the putative CK2 phosphorylation site negatively regulates the DNA binding activity of TGA2. Analysis of transgenic Arabidopsis overexpressing TGA2-GFP or TGA2-A-GFP, in the absence of SA treatment, revealed that they accumulated similarly elevated levels of PR-1 gene transcripts. Possible reasons why mutations in the putative CK2 phosphorylation site had little effect on PR-1 induction by TGA2 are discussed.
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