SLR1;OsGAI

Gene Details

MSU gene ID: LOC_Os03g49990
RAPdb gene ID: Os03g0707600
Gene Symbol: SLR1 OsGAI OsSLR1
Genome: MSU7 , IRGSP-1.0
Species: Oryza sativa

Functional Descriptions

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 degradation.
We identified a semidominant dwarf mutant, SLR1-d4, which contains a mutation in the region encoding the C-terminal GRAS domain of SLR1 (SLR1(G576V)).
Disturbing GA homeostasis affected the expression of the GA signaling genes GID1 (GIBBERELLIN INSENSITIVE DWARF 1), GID2 and SLR1.
GA perception by GID1 causes SLR1 protein degradation involving the F-box protein GID2; this triggers GA-associated responses such as shoot elongation and seed germination.
We also succeeded in producing GA-insensitive dwarf rice by transforming wild-type rice with a modified SLR1 gene construct that has a 17–amino acid deletion affecting the DELLA region.
Map-based cloning revealed that the dwarf phenotype in these mutants was caused by gain-of-function mutations in the N-terminal region of SLR1.
Isolation and characterization of dominant dwarf mutants, SLR1-d, in rice.
These results indicate that constitutive activation of the GA signal transduction pathway by the SLR1-1 mutation promotes the endogenous ABA level.
The slender rice (SLR1-1) mutant, carrying a lethal and recessive single mutation, has a constitutive gibberellin (GA)-response phenotype and behaves as if it were saturated with GAs [Ikeda et al.
Overexpression of SLR1 in wild-type plants caused a severe dwarf phenotype, which was significantly suppressed by EL1 deficiency, indicating the negative effect of SLR1 on GA signalling requires the EL1 function.
The enhanced expression of GA biosynthetic genes in dgl1 is not caused by inappropriate GA signaling because the expression of these genes was repressed by GA3 treatment, and degradation of the rice DELLA protein SLR1 was triggered by GA3 in this mutant.
The SLR1 gene, with sequence homology to members of the plant-specific GRAS gene family, is a mediator of the GA signal transduction process.
SLR1 maps to OsGAI in rice and has significant homology with height-regulating genes, such as RHT-1Da in wheat, D8 in maize, and GAI and RGA in Arabidopsis.
slender Rice, a Constitutive Gibberellin Response Mutant, Is Caused by a Null Mutation of the SLR1 Gene, an Ortholog of the Height-Regulating Gene GAI/RGA/RHT/D8.
Rice early flowering1, a CKI, phosphorylates DELLA protein SLR1 to negatively regulate gibberellin signalling.
When SLR1 proteins with various deletions were over-expressed in rice, the severity of dwarfism correlated with the transactivation activity observed in yeast, indicating that SLR1 suppresses plant growth through transactivation activity.
In GA-insensitive and GA biosynthesis mutants, SLENDER RICE1 (SLR1) accumulates to high levels, and the severity of dwarfism is usually correlated with the level of SLR1 accumulation.
An exception is the GA-insensitive F-box mutant gid2, which shows milder dwarfism than mutants such as gid1 and cps even though it accumulates higher levels of SLR1.
The level of SLR1 protein in gid2 was decreased by loss of GID1 function or treatment with a GA biosynthesis inhibitor, and dwarfism was enhanced.
Conversely, overproduction of GID1 or treatment with GA(3) increased the SLR1 level in gid2 and reduced dwarfism.
Further studies showed that the phosphorylation of SLR1 is important for maintaining its activity and stability, and mutation of the candidate phosphorylation site of SLR1 results in the altered GA signalling.
GID2, an F-box subunit of the SCF E3 complex, specifically interacts with phosphorylated SLR1 protein and regulates the gibberellin-dependent degradation of SLR1 in rice.
SLR1-GFP worked in nuclei to repress the GA signaling pathway; its overproduction caused a dwarf phenotype.
The rice SLR1 (SLENDER RICE 1) gene encodes a DELLA protein that belongs to a subfamily of the GRAS protein superfamily and that functions as a repressor of gibberellin (GA) signaling.
The rice SPINDLY gene functions as a negative regulator of gibberellin signaling by controlling the suppressive function of the DELLA protein, SLR1, and modulating brassinosteroid synthesis.
This indicates that the function of OsSPY in GA signaling is not via changes in the amount or stability of SLR1, but probably involves control of the suppressive function of SLR1.
The rice slender mutant (SLR1-1) is caused by a single recessive mutation and results in a constitutive gibberellin (GA) response phenotype.
Notably Sub1A increased the accumulation of the GA signaling repressors Slender Rice-1 (SLR1) and SLR1 Like-1 (SLRL1) and concomitantly diminished GA-inducible gene expression under submerged conditions.
Together, these results demonstrate that Sub1A limits ethylene-promoted GA responsiveness during submergence by augmenting accumulation of the GA signaling repressors SLR1 and SLRL1.
In the Sub1A overexpression line, SLR1 protein levels declined under prolonged submergence but were accompanied by an increase in accumulation of SLRL1, which lacks the DELLA domain.
Submergence tolerance conferred by Sub1A is mediated by SLR1 and SLRL1 restriction of gibberellin responses in rice.
These results indicate that the product of the SLR1 gene is an intermediate of the GA signal transduction pathway.
Furthermore, introduction of a 6-kb genomic DNA fragment containing the wild-type SLR1 gene into the SLR1-1 mutant restored GA sensitivity to normal.
Thus, we demonstrate opposite GA response phenotypes depending on the type of mutations in SLR1.
Application of GA(3) to SLR1-GFP overproducers induced GA actions such as shoot elongation, downregulation of GA 20-oxidase expression, and upregulation of SLR1 expression linked with the disappearance of the nuclear SLR1-GFP protein.
The rice (Oryza sativa) DELLA protein SLR1 acts as a repressor of gibberellin (GA) signaling.
Release of the repressive activity of rice DELLA protein SLR1 by gibberellin does not require SLR1 degradation in the gid2 mutant.
These results indicate that derepression of SLR1 repressive activity can be accomplished by GA and GID1 alone and does not require F-box (GID2) function.
Evidence for GA signaling without GID2 was also provided by the expression behavior of GA-regulated genes such as GA-20oxidase1, GID1, and SLR1 in the gid2 mutant.
The C-terminal GRAS domain of SLR1 also exhibits a suppressive function on plant growth, possibly by directly or indirectly interacting with the promoter region of target genes.
Based on the constitutive GA response phenotype of SLR1 mutants, SLR1 has been thought to be the sole DELLA-type protein suppressing GA signals in rice.
However, the repressive activity of SLRL1 against GA signaling was much weaker than a truncated SLR1 lacking the DELLA domain.
This activity was suppressed by the GA-dependent GID1-SLR1 interaction, which may explain why GA responses are induced in the presence of GA.
Our results indicate that the N-terminal region of SLR1 has two roles in GA signaling: interaction with GID1 and transactivation activity.
The slender rice1 mutant (SLR1) shows a constitutive gibberellin (GA) response phenotype.
Furthermore, apart from the alteration of expression levels of the gibberellin biosynthesis genes, accumulation of SLR1 protein was found in the overexpressing transgenic plants, indicating that the expression level of EUI1 is implicated in both gibberellin-mediated SLR1 destruction and a feedback regulation in gibberellin biosynthesis.
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.
The analyses revealed that the SLR1 protein can be divided into four parts: a GA signal perception domain located at the N terminus, a regulatory domain for its repression activity, a dimer formation domain essential for signal perception and repression activity, and a repression domain at the C terminus.
We conclude that GA signal transduction is regulated by the appearance or disappearance of the nuclear SLR1 protein, which is controlled by the upstream GA signal.
GA Perception and Signal Transduction: Molecular Interactions of the GA Receptor GID1 with GA and the DELLA Protein SLR1 in Rice.
Together these findings favor a model whereby SLR1 acts as a positive regulator of hemibiotroph resistance in rice by integrating and amplifying SA- and JA-dependent defense signaling.
Moreover, contrary to the differential effect of DELLA on the archetypal defense hormones salicylic acid (SA) and jasmonic acid (JA) in Arabidopsis, we demonstrate that the resistance-promoting effect of SLR1 is due at least in part to its ability to boost both SA- and JA-mediated rice defenses.
The DELLA protein SLR1 integrates and amplifies salicylic acid- and jasmonic acid-dependent innate immunity in rice.
In a reciprocal manner, we found JA and SA treatment to interfere with GA metabolism and stabilize SLR1.
<U+00A0>graminicola, and SLR1 plays a central role in the JA-mediated defense response in rice against this nematode.
Expression of SLR1 and five key GA biosynthetic genes were disturbed in SLR1-d6 and the interaction between SLR1-d6 and GID1 was decreased.
Characterization of a new semi-dominant dwarf allele of SLR1 and its potential application in hybrid rice breeding.
SLR1 inhibits MOC1 degradation to coordinate tiller number and plant height in rice.
This discovery provides a molecular explanation for the coordinated control of plant height and tiller number in rice by GAs, SLR1 and MOC1.
The protein levels of OsIDD2 were unaffected by GA in the wild type and OsIDD2OE plants, implying that OSIDD2 promotes the expression of miR396 and likely requires the coactivator of SLR1.
Furthermore, salt induces OsPIL14 turnover but enhances SLR1 accumulation.
OsGRAS39 was found to be a highly expressive gene under sheath blight infection and both abiotic stress treatments while OsGRAS8, OsSHR1 and OsSLR1 were also responsive.
SLR1-mediated broad-spectrum resistance was subverted by these independently evolved viral proteins, which all interrupted the functional crosstalk between SLR1 and jasmonic acid (JA) signaling.
Viral proteins encoded by different types of rice viruses all directly trigger the rapid degradation of SLR1 by promoting association with the GA receptor OsGID1.
Moreover, under the low-temperature (LT) condition, the osmkkk62/70 mutant had slightly higher Gibberellin (GA) contents, increased expression of GA biosynthesis genes, and lower protein level of OsSLR1 in anthers than those in WT.

Functional Keywords

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Gene Resources

Sequences

cDNA Sequence

>LOC_Os03g49990.1
GATGCCCTTCCTCTTCTCCCCCCTTGCTACTACTAGTTGCTTGCCTCTTCCCACCTCACCTCGCATTGCAATCTCGCATCGCCTCTTCCTTCTCTTCTTCCCCTTCTTCTCCCCTTCTCATCCAACCTCGCTTCCCAACCCTGGATCCAAATCCCAACCTATCCCAAAGCCGAAACCGAGGAGAGGAAAAAGGTTACGCGCAATTATTACTAGCTATAGCTAGGTAGGTTTGGGGGAGGCGAGATCATGAAGCGCGAGTACCAAGAAGCCGGCGGGAGCAGCGGCGGCGGGAGCAGCGCCGATATGGGGTCGTGCAAGGACAAGGTGATGGCGGGGGCGGCGGGGGAGGAGGAGGACGTCGACGAGCTGCTGGCGGCGCTCGGGTACAAGGTGCGGTCGTCCGACATGGCCGACGTCGCGCAGAAGCTGGAGCAGCTGGAGATGGCCATGGGGATGGGCGGCGTGAGCGCCCCCGGCGCCGCGGATGACGGGTTCGTGTCGCACCTGGCCACGGACACCGTGCACTACAACCCCTCGGACCTCTCCTCCTGGGTCGAGAGCATGCTTTCCGAGCTCAACGCGCCGCTGCCCCCTATCCCGCCAGCGCCGCCGGCTGCCCGCCATGCTTCCACCTCGTCCACTGTCACCGGCGGCGGTGGTAGCGGCTTCTTTGAACTCCCAGCCGCTGCCGACTCGTCGAGTAGCACCTACGCCCTCAGGCCGATCTCCTTACCGGTGGTGGCGACGGCTGACCCGTCGGCTGCTGACTCGGCGAGGGACACCAAGCGGATGCGCACTGGCGGCGGCAGCACGTCGTCGTCCTCATCGTCGTCTTCCTCTCTGGGCGGTGGGGCCTCGCGGGGCTCTGTGGTGGAGGCTGCTCCGCCGGCGACGCAAGGGGCCGCGGCGGCGAATGCGCCCGCCGTGCCGGTTGTGGTGGTTGACACGCAGGAGGCTGGGATCCGGCTGGTGCACGCGTTGCTGGCGTGCGCGGAGGCCGTGCAGCAGGAGAACTTCGCGGCCGCGGAGGCGCTGGTCAAGCAGATCCCCACGCTGGCCGCGTCCCAGGGCGGCGCCATGCGCAAGGTCGCTGCCTACTTCGGCGAGGCCCTCGCCCGCCGCGTGTACCGCTTCCGCCCCGCGGACAGCACCCTCCTCGACGCCGCCTTCGCCGACCTTCTGCACGCCCACTTCTACGAGTCCTGCCCCTACCTCAAGTTCGCCCACTTCACCGCAAATCAAGCCATCCTCGAGGCTTTCGCCGGCTGCCACCGCGTCCACGTCGTCGACTTCGGCATCAAGCAGGGGATGCAATGGCCAGCTCTCCTCCAGGCCCTCGCCCTTCGTCCCGGCGGCCCCCCATCGTTCCGCCTCACCGGCGTCGGCCCCCCGCAGCCGGACGAGACCGACGCCTTGCAGCAGGTGGGTTGGAAGCTTGCCCAGTTCGCGCACACCATTCGCGTCGACTTCCAGTACCGGGGACTCGTCGCCGCCACTCTCGCGGACTTGGAGCCGTTCATGCTGCAGCCGGAGGGCGAGGCGGACGCGAACGAGGAGCCTGAGGTGATCGCCGTCAACTCGGTGTTCGAGCTGCACCGGCTGCTCGCGCAGCCCGGCGCGCTGGAGAAGGTCCTGGGCACGGTGCACGCGGTGCGGCCAAGGATCGTCACCGTGGTAGAGCAGGAGGCCAACCACAACTCCGGCTCATTCCTCGACCGGTTCACCGAGTCGCTGCACTACTACTCCACCATGTTCGATTCCCTCGAGGGCGGCAGCTCCGGCCAGGCCGAGCTCTCTCCGCCGGCTGCCGGGGGCGGCGGTGGCACGGACCAGGTCATGTCCGAGGTGTACCTCGGCCGGCAGATCTGCAACGTCGTGGCGTGCGAGGGCGCGGAGCGCACGGAGCGCCACGAGACGCTGGGGCAGTGGCGCAACCGCCTCGGCCGCGCCGGCTTCGAGCCCGTGCACCTGGGCTCCAATGCCTACAAACAGGCGAGCACGCTCCTCGCGCTTTTCGCCGGCGGCGACGGCTACCGGGTGGAGGAGAAGGAGGGCTGCCTCACGCTGGGCTGGCACACGCGCCCGCTCATCGCCACCTCGGCATGGCGCGTCGCCGCGGCGTGATCGCAAAGTTTTTGGGACGCTGCACCACGTGTTTGCCGCCGATCACGGCGCGACCCCCCCCCCCCCCCCTCTCTCTCTCCCCGGCTCACCGGCGGCACAATTGAAGCTTGACGTCAACGAACGCTCAATTGCAGCGACCGATCGGGCTTACGGTTCTCGCCGGCGTGAAGAGATCGACGACTGGACTCCGACCAGACCGACGGCTTGTTCGTTCTCCTTTCCCAATTACCCCGTTCCTTGGTCCTCCTAGCCCATCTATTATGTTTAAATGTCAATTATTATGTGTAATTTCTCCAATCGCTCATATTAAATAAGGACGAACCGAACTGGATTTCATTAGCTCCAATGAGAATTTTGTATACAAGGCACCGATCTAAAAATTGAGCTATATGTTCATGAGTTACAGAATGCCCCCTTGATGCTCCTGTGAA

CDS Sequence

>LOC_Os03g49990.1
ATGAAGCGCGAGTACCAAGAAGCCGGCGGGAGCAGCGGCGGCGGGAGCAGCGCCGATATGGGGTCGTGCAAGGACAAGGTGATGGCGGGGGCGGCGGGGGAGGAGGAGGACGTCGACGAGCTGCTGGCGGCGCTCGGGTACAAGGTGCGGTCGTCCGACATGGCCGACGTCGCGCAGAAGCTGGAGCAGCTGGAGATGGCCATGGGGATGGGCGGCGTGAGCGCCCCCGGCGCCGCGGATGACGGGTTCGTGTCGCACCTGGCCACGGACACCGTGCACTACAACCCCTCGGACCTCTCCTCCTGGGTCGAGAGCATGCTTTCCGAGCTCAACGCGCCGCTGCCCCCTATCCCGCCAGCGCCGCCGGCTGCCCGCCATGCTTCCACCTCGTCCACTGTCACCGGCGGCGGTGGTAGCGGCTTCTTTGAACTCCCAGCCGCTGCCGACTCGTCGAGTAGCACCTACGCCCTCAGGCCGATCTCCTTACCGGTGGTGGCGACGGCTGACCCGTCGGCTGCTGACTCGGCGAGGGACACCAAGCGGATGCGCACTGGCGGCGGCAGCACGTCGTCGTCCTCATCGTCGTCTTCCTCTCTGGGCGGTGGGGCCTCGCGGGGCTCTGTGGTGGAGGCTGCTCCGCCGGCGACGCAAGGGGCCGCGGCGGCGAATGCGCCCGCCGTGCCGGTTGTGGTGGTTGACACGCAGGAGGCTGGGATCCGGCTGGTGCACGCGTTGCTGGCGTGCGCGGAGGCCGTGCAGCAGGAGAACTTCGCGGCCGCGGAGGCGCTGGTCAAGCAGATCCCCACGCTGGCCGCGTCCCAGGGCGGCGCCATGCGCAAGGTCGCTGCCTACTTCGGCGAGGCCCTCGCCCGCCGCGTGTACCGCTTCCGCCCCGCGGACAGCACCCTCCTCGACGCCGCCTTCGCCGACCTTCTGCACGCCCACTTCTACGAGTCCTGCCCCTACCTCAAGTTCGCCCACTTCACCGCAAATCAAGCCATCCTCGAGGCTTTCGCCGGCTGCCACCGCGTCCACGTCGTCGACTTCGGCATCAAGCAGGGGATGCAATGGCCAGCTCTCCTCCAGGCCCTCGCCCTTCGTCCCGGCGGCCCCCCATCGTTCCGCCTCACCGGCGTCGGCCCCCCGCAGCCGGACGAGACCGACGCCTTGCAGCAGGTGGGTTGGAAGCTTGCCCAGTTCGCGCACACCATTCGCGTCGACTTCCAGTACCGGGGACTCGTCGCCGCCACTCTCGCGGACTTGGAGCCGTTCATGCTGCAGCCGGAGGGCGAGGCGGACGCGAACGAGGAGCCTGAGGTGATCGCCGTCAACTCGGTGTTCGAGCTGCACCGGCTGCTCGCGCAGCCCGGCGCGCTGGAGAAGGTCCTGGGCACGGTGCACGCGGTGCGGCCAAGGATCGTCACCGTGGTAGAGCAGGAGGCCAACCACAACTCCGGCTCATTCCTCGACCGGTTCACCGAGTCGCTGCACTACTACTCCACCATGTTCGATTCCCTCGAGGGCGGCAGCTCCGGCCAGGCCGAGCTCTCTCCGCCGGCTGCCGGGGGCGGCGGTGGCACGGACCAGGTCATGTCCGAGGTGTACCTCGGCCGGCAGATCTGCAACGTCGTGGCGTGCGAGGGCGCGGAGCGCACGGAGCGCCACGAGACGCTGGGGCAGTGGCGCAACCGCCTCGGCCGCGCCGGCTTCGAGCCCGTGCACCTGGGCTCCAATGCCTACAAACAGGCGAGCACGCTCCTCGCGCTTTTCGCCGGCGGCGACGGCTACCGGGTGGAGGAGAAGGAGGGCTGCCTCACGCTGGGCTGGCACACGCGCCCGCTCATCGCCACCTCGGCATGGCGCGTCGCCGCGGCGTGA

Protein Sequence

>LOC_Os03g49990.1
MKREYQEAGGSSGGGSSADMGSCKDKVMAGAAGEEEDVDELLAALGYKVRSSDMADVAQKLEQLEMAMGMGGVSAPGAADDGFVSHLATDTVHYNPSDLSSWVESMLSELNAPLPPIPPAPPAARHASTSSTVTGGGGSGFFELPAAADSSSSTYALRPISLPVVATADPSAADSARDTKRMRTGGGSTSSSSSSSSSLGGGASRGSVVEAAPPATQGAAAANAPAVPVVVVDTQEAGIRLVHALLACAEAVQQENFAAAEALVKQIPTLAASQGGAMRKVAAYFGEALARRVYRFRPADSTLLDAAFADLLHAHFYESCPYLKFAHFTANQAILEAFAGCHRVHVVDFGIKQGMQWPALLQALALRPGGPPSFRLTGVGPPQPDETDALQQVGWKLAQFAHTIRVDFQYRGLVAATLADLEPFMLQPEGEADANEEPEVIAVNSVFELHRLLAQPGALEKVLGTVHAVRPRIVTVVEQEANHNSGSFLDRFTESLHYYSTMFDSLEGGSSGQAELSPPAAGGGGGTDQVMSEVYLGRQICNVVACEGAERTERHETLGQWRNRLGRAGFEPVHLGSNAYKQASTLLALFAGGDGYRVEEKEGCLTLGWHTRPLIATSAWRVAAA*