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The Arabidopsis Mutant sleepy1gar2-1 Protein Promotes Plant Growth by Increasing the Affinity of the SCFSLY1 E3 Ubiquitin Ligase for DELLA Protein Substrates[W]
Open accessAbstract
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.
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Metadata
- Authors
- Fu, X., Richards, D. E., Fleck, B., Xie, D., Burton, N., & Harberd, N. P.
- Venue
- The Plant Cell
- Publisher
- Oxford University Press (OUP)
- Published
- 2004-06-01
- Volume
- 16
- Issue
- 6
- Pages
- 1406-1418
- ISSN
- 1040-4651 (ISSN-L)
- 1532-298X
- OpenAlex
- W2108097646
- Cited by
- 295
- References
- 52
- FWCI
- 20.24
- Type
- journal article
- Language
- en
- Open access
- bronze
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