The Arabidopsis Mutant sleepy1gar2-1 Protein Promotes Plant Growth by Increasing the Affinity of the SCFSLY1 E3 Ubiquitin Ligase for DELLA Protein Substrates[W]
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- Xiangdong Fu
- John Innes Centre, Norwich NR4 7UH, United Kingdom
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- Donald E. Richards
- John Innes Centre, Norwich NR4 7UH, United Kingdom
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- Barbara Fleck
- John Innes Centre, Norwich NR4 7UH, United Kingdom
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- Daoxin Xie
- Institute of Molecular and Cell Biology, Singapore 117609
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- Nicolas Burton
- John Innes Centre, Norwich NR4 7UH, United Kingdom
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- Nicholas P. Harberd
- John Innes Centre, Norwich NR4 7UH, United Kingdom
抄録
<jats:title>Abstract</jats:title><jats:p>DELLA proteins restrain the cell proliferation and enlargement that characterizes the growth of plant organs. Gibberellin stimulates growth via 26S proteasome–dependent destruction of DELLAs, thus relieving DELLA-mediated growth restraint. Here, we show that the Arabidopsis thaliana sleepy1gar2-1 (sly1gar2-1) mutant allele encodes a mutant subunit (sly1gar2-1) of an SCFSLY1 E3 ubiquitin ligase complex. SLY1 (the wild-type form) and sly1gar2-1 both confer substrate specificity on this complex via specific binding to the DELLA proteins. However, sly1gar2-1 interacts more strongly with the DELLA target than does SLY1. In addition, the strength of the SCFSLY1–DELLA interaction is increased by target phosphorylation. Growth-promoting DELLA destruction is dependent on SLY1 availability, on the strength of the interaction between SLY1 and the DELLA target, and on promotion of the SCFSLY1–DELLA interaction by DELLA phosphorylation.</jats:p>
収録刊行物
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- The Plant Cell
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The Plant Cell 16 (6), 1406-1418, 2004-06-01
Oxford University Press (OUP)
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詳細情報
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- CRID
- 1360574095802340224
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- NII論文ID
- 80016747670
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- ISSN
- 1532298X
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- データソース種別
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