Os05g0407500
The rice gibberellin-insensitive dwarf1 (gid1) gene is well known as a soluble receptor mediating GA signalling in rice and affects the plant height of rice.
Contents
Annotated Information
Function
Gibberellin-insensitive dwarf1 (gid1), a recessive gibberellin (GA)-insensitive dwarf mutant of rice, shows a severe dwarf phenotype and contains high concentrations of endogenous GA (Tanaka et al., 2006). GID1 is a soluble receptor mediating GA signalling in rice, and it encodes an unknown protein with similarity to the hormone-sensitive lipases; preferential localization of a GID1–green fluorescent protein (GFP) signal in nuclei (Miyako et al., 2005). A gid1-1/slr1-1 double mutant exhibited the slr1-1 phenotype, indicating that GID1 and SLR1 function in the same GA signalling pathway and that SLR1 is epistatic to GID1 (Miyako et al., 2005). Among the proteins hyper-accumulated in gid1 were osmotin, triosephosphate isomerase, probenazole inducible protein (PBZ1) and pathogenesis-related protein 10.Gid1 is involved intolerance to cold stress and resistance to blast fungus (Tanaka et al., 2006).
Expression
The GID1 gene contains one intron and two exons, and encodes a 354-amino-acid polypeptide (Miyako et al., 2005).GID1 overexpression resulted in a GA-hypersensitive phenotype (Miyako et al., 2005). Expression of this gene was enhanced in shoots of the wild type by cold stress or by rice blast fungus infection. The entcopalyl diphosphate synthase (OsCPS) genes, which encode enzymes at the branch point between GA and phytoalexin biosynthesis, were expressed differentially in gid1relative to the wild type. Specifically, OsCPS1, which encodes an enzyme in the GA biosynthesis pathway, was down-regulated and OsCPS2 and OsCPS4, which encode enzymes in phytoalexin biosynthesis, were up-regulated in gid1 (Tanaka et al., 2006)
Evolution
A database search revealed that there is no gene homologous to GID1 in rice, whereas there are three homologues in Arabidopsis, which are annotated as unknown proteins. However, an NCBI Conserved Domain Search indicated that GID1shares homology with the consensus sequence of the hormonesensitive lipase (HSL) family19, including the conserved HSL motifs HGG and GXSXG (Miyako et al., 2005). According to EST sequences, amino acid sequences coding these genes w ere deduced in sorghum, wheat maize (G ID1A and G ID1B) and cotton. Their amino acid sequences had higher similarity to rice with 81.44%, 81.36%, 80.50%, 79.14%, 63.13%, respectively (Sui Jiong-ming, 2009).
Knowledge Extension
The GID1-GA complex directly interacts with SLENDER RICE1 (SLR1), a DELLA repressor protein in GA signaling. GA4 has the highest affinity to GID1 and is the most effective form of GA in planta. The DELLA and TVHYNP domains of SLR1 are required for the GID1–SLR1 interaction. The amino acid residues important for SLR1 interaction completely overlapped the residues required for GA binding that were scattered throughout the GID1 molecule. When these residues were plotted on the GID1 structure predicted by analogy with HSL tertiary structure, many residues were located at regions corresponding to the substrate binding pocket and lid. Furthermore, the GA–GID1 interaction was stabilized by SLR1 (Miyako et al., 2007). The DELLA protein SLENDER RICE1 (SLR1) is a repressor of gibberellin (GA) signaling in rice (Oryza sativa), and most of the GA-associated responses are induced upon SLR1 degradation. It is assumed that interaction between gibberellin-insensitive dwarf1 (GID1) and the N-terminal DELLA/TVHYNP motif of SLR1 triggers F-box protein GID2-mediated SLR1. Surface plasmon resonance of GID1-SLR1 and GID1-SLR1G576V interactions revealed that the GRAS domain of SLR1 functions to stabilize the GID1-SLR1 interaction by reducing its dissociation rate and that the G576V substitution in SLR1diminishes this stability degradation. when the DELLA/TVHYNP motif of SLR1 binds with GID1, it enables the GRAS domain of SLR1 to interact with GID1 and that the stable GID1-SLR1 complex is efficiently recognized by GID2 (Hirano et al., 2010). In vascular plants, phytohormone GA, receptor GID1, and repressor DELLA shape the GA– GID1–DELLA module in GA signaling cascade. Sequence reshuffling, functional divergence, and adaptive selection are main driving forces during the evolution of GA path¬way components. The GA–GID1–DELLA complex inter¬acts with second messengers and other plant hormones to integrate environmental and endogenous cues, which is beneficial to phytohormones homeostasis and other bio¬logical events（Wang and Deng, 2014）.
Labs working on this gene
Bioscience and Biotechnology Center, Nagoya University, Nagoya 464-8601, Japan
BioResources Center, Riken, Tsukuba 305-0074, Japan
College of Life Science, QAU, Qingdao 266109, China
Department of Biotechnology, Maebashi Institute of Technology, Gunma 371-0816, Japan
Department of Structural Biology, Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan
Department of Applied Biological Chemistry, The University of Tokyo, Tokyo 113-8657, Japan
Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan
Institute of Botany Academia, Sinica, Taipei 11529, Taiwan
Key Laboratory of Crop Genetics and Physiology of Jiangsu Province, Key Laboratory of Plant Functional Genomics of Ministry of Education, Yangzhou University, Yangzhou 225009, China
National Institute of Agrobiological Sciences, Tsukuba 305-8602, Japan
References
Hirano, K., Asano, K., Tsuji, H., Kawamura, M., Mori, H., Kitano, H., ... & Matsuoka, M. (2010). Characterization of the molecular mechanism underlying gibberellin perception complex formation in rice. The Plant Cell Online, 22(8), 2680-2696.
Sui Jiong-ming. (2009). Homologous comparison of GA acceptor among several crops(Chinese version with English abstract). Journal of Qingdao Agricultural University (Natural Science), 26(4): 309~ 312, 2009.
Tanaka, N., Matsuoka, M., Kitano, H., Asano, T., Kaku, H., & Komatsu, S. (2006). gid1, a gibberellin‐insensitive dwarf mutant, shows altered regulation of probenazole‐inducible protein (PBZ1) in response to cold stress and pathogen attack. Plant, cell & environment, 29(4), 619-631.
Ueguchi-Tanaka, M., Ashikari, M., Nakajima, M., Itoh, H., Katoh, E., Kobayashi, M., ... & Matsuoka, M. (2005). Gibberellin insensitive dwarf1 encodes a soluble receptor for gibberellin. Nature, 437(7059), 693-698.
Ueguchi-Tanaka, M., Nakajima, M., Katoh, E., Ohmiya, H., Asano, K., Saji, S., ... & Matsuoka, M. (2007). Molecular interactions of a soluble gibberellin receptor, GID1, with a rice DELLA protein, SLR1, and gibberellin. The Plant Cell Online, 19(7), 2140-2155.
Wang, Y., & Deng, D. (2013). Molecular basis and evolutionary pattern of GA–GID1–DELLA regulatory module. Molecular Genetics and Genomics, 1-9.
Yamamoto, Y., Hirai, T., Yamamoto, E., Kawamura, M., Sato, T., Kitano, H., ... & Ueguchi-Tanaka, M. (2010). A rice gid1 suppressor mutant reveals that gibberellin is not always required for interaction between its receptor, GID1, and DELLA proteins. The Plant Cell Online, 22(11), 3589-3602.
