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Arabidopsis OSMOTIN 34 Functions in the ABA Signaling Pathway and Is Regulated by Proteolysis.
Park, Eun-Joo; Kim, Tae-Houn.
Affiliation
  • Park EJ; Department of Bio-Health Convergence, Duksung Women's University, Seoul 01369, Korea.
  • Kim TH; Department of Bio-Health Convergence, Duksung Women's University, Seoul 01369, Korea.
Int J Mol Sci ; 22(15)2021 Jul 24.
Article in En | MEDLINE | ID: mdl-34360680
ABSTRACT
Plants have evolutionarily established resistance responses to a variety of abiotic stress conditions, in which ABA mediates the integrated regulation of these stress responses. Numerous proteins function at the transcription level or at the protein level when contributing to controls of the ABA signaling process. Although osmotin is identified as a salt-inducible protein, its function in the abiotic stress response is yet to be elucidated. To examine the role of Arabidopsis OSMOTIN 34 (OSM34) in the ABA signaling pathway, a deletion mutant osm34 generated by a CRISPR/Cas9 system and the double mutant osm34 osml (osmotin 34-like) were analyzed for various ABA responses. Both osm34 and osm34 osml showed reduced levels of ABA responses in seeds and leaves. Moreover, proline level and expression of the proline biosynthesis gene P5CS1 was significantly reduced in osm34 osml. Interestingly, OSM34 binds to SKP2A, an F-Box protein whose transcription is induced by ABA. The protein stability of OSM34 was determined to be under the control of the 26S proteasome. In conclusion, our data suggest that OSM34 functions as a positive regulator in the generation of ABA responses and is under post-translational control.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Stress, Physiological / Signal Transduction / Arabidopsis / Abscisic Acid / Arabidopsis Proteins Language: En Journal: Int J Mol Sci Year: 2021 Document type: Article

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Stress, Physiological / Signal Transduction / Arabidopsis / Abscisic Acid / Arabidopsis Proteins Language: En Journal: Int J Mol Sci Year: 2021 Document type: Article