Journal
PLANT CELL
Volume 16, Issue 6, Pages 1406-1418Publisher
AMER SOC PLANT BIOLOGISTS
DOI: 10.1105/tpc.021386
Keywords
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Funding
- Biotechnology and Biological Sciences Research Council [BBS/E/J/00000583] Funding Source: researchfish
- Biotechnology and Biological Sciences Research Council [BBS/E/J/00000583] Funding Source: Medline
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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 sleepy1(gar2-1) (Sly1(gar2-1)) mutant allele encodes a mutant subunit (sly1(gar2-1)) of an SCFSLY1 E3 ubiquitin ligase complex. SLY1 (the wild-type form) and Sly1(gar2-1) both confer substrate specificity on this complex via specific binding to the DELLA proteins. However, sly1(gar2-1) 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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