Gibberellin-mediated proteasome-dependent degradation of the barley DELLA protein SLN1 repressor
| Autor: | Jinrong Peng, Tahar Ait-Ali, Donald Ernest Richards, Nicholas P. Harberd, Xiangdong Fu, Helen J. Ougham, Llewelyn W. Hynes |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2002 |
| Předmět: |
Proteasome Endopeptidase Complex
Phosphatase Repressor Plant Science Biology Protein degradation Dephosphorylation Aprotinin Multienzyme Complexes Okadaic Acid Protein phosphorylation Sulfones Enzyme Inhibitors Protein kinase A Alleles Derepression Plant Proteins Hordeum Cell Biology Gibberellins Phenylmethylsulfonyl Fluoride Plant Leaves Cysteine Endopeptidases Biochemistry Enzyme Induction Mutation Seeds Vanadates alpha-Amylases Signal transduction Signal Transduction Research Article |
| Zdroj: | The Plant cell. 14(12) |
| ISSN: | 1532-298X 1040-4651 |
| Popis: | DELLA proteins are nuclear repressors of plant gibberellin (GA) responses. Here, we investigate the properties of SLN1, a DELLA protein from barley that is destabilized by GA treatment. Using specific inhibitors of proteasome function, we show that proteasome-mediated protein degradation is necessary for GA-mediated destabilization of SLN1. We also show that GA responses, such as the aleurone alpha-amylase response and seedling leaf extension growth, require proteasome-dependent GA-mediated SLN1 destabilization. In further experiments with protein kinase and protein phosphatase inhibitors, we identify two additional signaling steps that are necessary for GA response and for GA-mediated destabilization of SLN1. Thus, GA signaling involves protein phosphorylation and dephosphorylation steps and promotes the derepression of GA responses via proteasome-dependent destabilization of DELLA repressors. |
| Databáze: | OpenAIRE |
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