Transcriptional regulator DELLA protein N terminal
SMART accession number:
SM01129
Description:
Gibberellins are plant hormones which have great impact on growth signalling. DELLA proteins are transcriptional regulators of growth related proteins which are downregulated when gibberellins bind to their receptor GID1. GID1 forms a complex with DELLA proteins and signals them towards 26S proteasome. The N terminal of DELLA proteins contains conserved DELLA and VHYNP motifs which are important for GID1 binding and proteolysis of the DELLA proteins. ((PUBMED:19037309))
Family alignment:
There are 604 DELLA domains in 604 proteins in SMART's nrdb database.
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Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing DELLA domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with DELLA domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing DELLA domain in the selected taxonomic class.
Gibberellin-induced DELLA recognition by the gibberellin receptor GID1.
Nature. 2008; 456: 459-63
Display abstract
Gibberellins control a range of growth and developmental processes in higherplants and have been widely used in the agricultural industry. By binding to anuclear receptor, GIBBERELLIN INSENSITIVE DWARF1 (GID1), gibberellins regulategene expression by promoting degradation of the transcriptional regulator DELLAproteins, including GIBBERELLIN INSENSITIVE (GAI). The precise manner in whichGID1 discriminates and becomes activated by bioactive gibberellins for specificbinding to DELLA proteins remains unclear. Here we present the crystal structure of a ternary complex of Arabidopsis thaliana GID1A, a bioactive gibberellin andthe amino-terminal DELLA domain of GAI. In this complex, GID1A occludesgibberellin in a deep binding pocket covered by its N-terminal helical switchregion, which in turn interacts with the DELLA domain containing DELLA, VHYNP andLExLE motifs. Our results establish a structural model of a plant hormonereceptor that is distinct from the mechanism of the hormone perception andeffector recognition of the known auxin receptors.
