2zsh
From Proteopedia
Structural basis of gibberellin(GA3)-induced DELLA recognition by the gibberellin receptor
Structural highlights
Function[GID1A_ARATH] Functions as soluble gibberellin (GA) receptor. GA is an essential hormone that regulates growth and development in plants. Binds with high affinity the biologically active gibberellin GA4, but has no affinity for the biologically inactive GAs. In response to GA, interacts with specific DELLA proteins, known as repressors of GA-induced growth, and targets them for degradation via proteasome. Seems to be required for GA signaling that controls root growth, seed germination, stem elongation and flower development. Partially redundant with GID1B and GID1C.[1] [2] [3] [GAI_ARATH] Probable transcriptional regulator that acts as a repressor of the gibberellin (GA) signaling pathway. No effect of the BOI proteins on its stability. Probably acts by participating in large multiprotein complexes that repress transcription of GA-inducible genes. Positively regulates XERICO expression. In contrast to RGA, it is less sensitive to GA. Its activity is probably regulated by other phytohormones such as auxin and ethylene.[4] [5] [6] [7] [8] [9] [10] [11] Publication Abstract from PubMedGibberellins control a range of growth and developmental processes in higher plants and have been widely used in the agricultural industry. By binding to a nuclear receptor, GIBBERELLIN INSENSITIVE DWARF1 (GID1), gibberellins regulate gene expression by promoting degradation of the transcriptional regulator DELLA proteins, including GIBBERELLIN INSENSITIVE (GAI). The precise manner in which GID1 discriminates and becomes activated by bioactive gibberellins for specific binding to DELLA proteins remains unclear. Here we present the crystal structure of a ternary complex of Arabidopsis thaliana GID1A, a bioactive gibberellin and the amino-terminal DELLA domain of GAI. In this complex, GID1A occludes gibberellin in a deep binding pocket covered by its N-terminal helical switch region, which in turn interacts with the DELLA domain containing DELLA, VHYNP and LExLE motifs. Our results establish a structural model of a plant hormone receptor that is distinct from the mechanism of the hormone perception and effector recognition of the known auxin receptors. Gibberellin-induced DELLA recognition by the gibberellin receptor GID1.,Murase K, Hirano Y, Sun TP, Hakoshima T Nature. 2008 Nov 27;456(7221):459-63. PMID:19037309[12] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Arath | Large Structures | Hakoshima, T | Hirano, Y | Murase, K | Sun, T P | Della | Developmental protein | Gibberellin | Gibberellin signaling pathway | Hormone receptor | Hydrolase | Nucleus | Phosphoprotein | Plant hormone receptor | Receptor | Repressor | Transcription | Transcription regulation | Ubl conjugation
