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Plant Cell Advance Online Publication
Published on December 28, 2006; 10.1105/tpc.106.047415

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Received September 15, 2006
Returned for revision November 7, 2006
Accepted November 17, 2006

Genetic Characterization and Functional Analysis of the GID1 Gibberellin Receptors in Arabidopsis

Jayne Griffiths 1, Kohji Murase 2, Ivo Rieu 1, Rodolfo Zentella 2, Zhong-Lin Zhang 2, Stephen J. Powers 1, Fan Gong 1, Andrew L. Phillips 1, Peter Hedden 1, Tai-ping Sun 2*, and Stephen G. Thomas 1

1 Rothamsted Research, Harpenden, Hertfordshire, AL5 2JQ, United Kingdom
2 Department of Biology, Duke University, Durham, North Carolina 27708-1000

* To whom correspondence should be addressed. E-mail: tps{at}duke.edu.

We investigated the physiological function of three Arabidopsis thaliana homologs of the gibberellin (GA) receptor GIBBERELLIN-INSENSITIVE DWARF1 (GID1) by determining the developmental consequences of GID1 inactivation in insertion mutants. Although single mutants developed normally, gid1a gid1c and gid1a gid1b displayed reduced stem height and lower male fertility, respectively, indicating some functional specificity. The triple mutant displayed a dwarf phenotype more severe than that of the extreme GA-deficient mutant ga1-3. Flower formation occurred in long days but was delayed, with severe defects in floral organ development. The triple mutant did not respond to applied GA. All three GID1 homologs were expressed in most tissues throughout development but differed in expression level. GA treatment reduced transcript abundance for all three GID1 genes, suggesting feedback regulation. The DELLA protein REPRESSOR OF ga1-3 (RGA) accumulated in the triple mutant, whose phenotype could be partially rescued by loss of RGA function. Yeast two-hybrid and in vitro pull-down assays confirmed that GA enhances the interaction between GID1 and DELLA proteins. In addition, the N-terminal sequence containing the DELLA domain is necessary for GID1 binding. Furthermore, yeast three-hybrid assays showed that the GA-GID1 complex promotes the interaction between RGA and the F-box protein SLY1, a component of the SCFSLY1 E3 ubiquitin ligase that targets the DELLA protein for degradation.




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