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Score: 16.00 |
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| Title: Characterization of the molecular mechanism underlying gibberellin perception complex formation in rice .
| | Author: Hirano K Asano K Tsuji H Kawamura M Mori H Kitano H Ueguchi-Tanaka M Matsuoka M | | Journal: Plant Cell Citation: V : 22 P : 2680-96 Year: 2010 Type: MEDLINE | | Literature: oryza Field: abstract Doc ID: pub20716699 Accession (PMID): 20716699 | | Abstract: 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 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 ) ) .
The GA-dependent degradation of SLR1 ( G576V ) was reduced in Slr1-d4 , and compared with SLR1 , SLR1 ( G576V ) showed reduced interaction with GID1 and almost none with GID2 when tested in yeast cells .
Surface plasmon resonance of GID1-SLR1 and GID1-SLR1 ( G576V ) 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 SLR1 diminishes this stability .
These results suggest that the stable interaction of GID1-SLR1 through the GRAS domain is essential for the recognition of SLR1 by GID2 .
We propose that 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 .
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[ Sen. 4, subscore: 4.00 ]: The GA-dependent degradation of SLR1 ( G576V ) was reduced in Slr1-d4 , and compared with SLR1 , SLR1 ( G576V ) showed reduced interaction with GID1 and almost none with GID2 when tested in yeast cells .
[ Sen. 3, subscore: 3.00 ]: 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 ) ) .
[ Sen. 1, subscore: 2.00 ]: 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 .
[ Sen. 2, subscore: 2.00 ]: 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 .
[ Sen. 5, subscore: 2.00 ]: Surface plasmon resonance of GID1-SLR1 and GID1-SLR1 ( G576V ) 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 SLR1 diminishes this stability .
[ Sen. 7, subscore: 2.00 ]: We propose that 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 .
[ Sen. 6, subscore: 1.00 ]: These results suggest that the stable interaction of GID1-SLR1 through the GRAS domain is essential for the recognition of SLR1 by GID2 .
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Score: 12.00 |
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| Title: The gibberellin signaling pathway is regulated by the appearance and disappearance of SLENDER RICE1 in nuclei .
| | Author: Itoh H Ueguchi-Tanaka M Sato Y Ashikari M Matsuoka M | | Journal: Plant Cell Citation: V : 14 ( 1 ) P : 57-70 Year: 2002 Type: ARTICLE | | Literature: oryza Field: abstract Doc ID: pub11826299 Accession (PMID): 11826299 | | Abstract: The slender rice1 mutant ( slr1 ) shows a constitutive gibberellin ( GA ) response phenotype .
To investigate the mode of action of SLR1 , we generated transgenic rice expressing a fusion protein consisting of SLR1 and green fluorescent protein ( SLR1-GFP ) and analyzed the phenotype of the transformants and the subcellular localization of GFP in vivo .
SLR1-GFP worked in nuclei to repress the GA signaling pathway ; its overproduction caused a dwarf phenotype .
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 .
We also performed domain analyses of SLR1 using transgenic plants overproducing different kinds of truncated SLR1 proteins .
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 | Matching Sentences:
[ Sen. 2, subscore: 3.00 ]: To investigate the mode of action of SLR1 , we generated transgenic rice expressing a fusion protein consisting of SLR1 and green fluorescent protein ( SLR1-GFP ) and analyzed the phenotype of the transformants and the subcellular localization of GFP in vivo .
[ Sen. 4, subscore: 3.00 ]: 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 .
[ Sen. 5, subscore: 2.00 ]: We also performed domain analyses of SLR1 using transgenic plants overproducing different kinds of truncated SLR1 proteins .
[ Sen. 1, subscore: 1.00 ]: The slender rice1 mutant ( slr1 ) shows a constitutive gibberellin ( GA ) response phenotype .
[ Sen. 3, subscore: 1.00 ]: SLR1-GFP worked in nuclei to repress the GA signaling pathway ; its overproduction caused a dwarf phenotype .
[ Sen. 6, subscore: 1.00 ]: 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 .
[ Sen. 7, subscore: 1.00 ]: 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
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Score: 10.00 |
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| Title: 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 .
| | Author: Ikeda A Ueguchi-Tanaka M Sonoda Y Kitano H Koshioka M Futsuhara Y Matsuoka M Yamaguchi J | | Journal: Plant Cell Citation: V : 13 ( 5 ) P : 999-1010 Year: 2001 Type: ARTICLE | | Literature: oryza Field: abstract Doc ID: pub11340177 Accession (PMID): 11340177 | | Abstract: The rice slender mutant ( slr1-1 ) is caused by a single recessive mutation and results in a constitutive gibberellin ( GA ) response phenotype .
The mutant elongates as if saturated with GAs .
In this mutant , ( 1 ) elongation was unaffected by an inhibitor of GA biosynthesis , ( 2 ) GA-inducible alpha-amylase was produced by the aleurone layers without gibberellic acid application , and ( 3 ) endogenous GA content was lower than in the wild-type plant .
These results indicate that the product of the SLR1 gene is an intermediate of the GA signal transduction pathway .
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 .
The GAI gene family is likely to encode transcriptional factors belonging to the GRAS gene superfamily .
DNA sequence analysis revealed that the slr1-1 mutation is a single basepair deletion of the nuclear localization signal domain , resulting in a frameshift mutation that abolishes protein production .
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 These results indicate that the slr1-1 mutant is caused by a loss-of-function mutation of the SLR1 gene , which is an ortholog of GAI , RGA , RHT , and D8 .
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 .
Thus , we demonstrate opposite GA response phenotypes depending on the type of mutations in SLR1 . | Matching Sentences:
[ Sen. 8, subscore: 4.00 ]: 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 These results indicate that the slr1-1 mutant is caused by a loss-of-function mutation of the SLR1 gene , which is an ortholog of GAI , RGA , RHT , and D8 .
[ Sen. 1, subscore: 1.00 ]: The rice slender mutant ( slr1-1 ) is caused by a single recessive mutation and results in a constitutive gibberellin ( GA ) response phenotype .
[ Sen. 4, subscore: 1.00 ]: These results indicate that the product of the SLR1 gene is an intermediate of the GA signal transduction pathway .
[ Sen. 5, subscore: 1.00 ]: 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 .
[ Sen. 7, subscore: 1.00 ]: DNA sequence analysis revealed that the slr1-1 mutation is a single basepair deletion of the nuclear localization signal domain , resulting in a frameshift mutation that abolishes protein production .
[ Sen. 9, subscore: 1.00 ]: 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 .
[ Sen. 10, subscore: 1.00 ]: Thus , we demonstrate opposite GA response phenotypes depending on the type of mutations in SLR1 .
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Score: 10.00 |
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| Title: Dissection of the phosphorylation of rice DELLA protein , SLENDER RICE1 .
| | Author: Itoh H Sasaki A Ueguchi-Tanaka M Ishiyama K Kobayashi M Hasegawa Y Minami E Ashikari M Matsuoka M | | Journal: Plant Cell Physiol .
Citation: V : 46 ( 8 ) P : 1392-9 Year: 2005 Type: ARTICLE | | Literature: oryza Field: abstract Doc ID: pub15979983 Accession (PMID): 15979983 | | Abstract: DELLA proteins are repressors of gibberellin signaling in plants .
Our previous studies have indicated that gibberellin signaling is derepressed by SCF ( GID2 ) -mediated proteolysis of the DELLA protein , SLENDER RICE1 ( SLR1 ) , in rice .
In addition , the gibberellin-dependent increase of phosphorylated SLR1 in the loss-of-function gid2 mutant suggests that the SCF ( GID2 ) -mediated degradation of SLR1 might be initiated by gibberellin-dependent phosphorylation .
To confirm the role of phosphorylation of SLR1 in its gibberellin-dependent degradation , we revealed that SLR1 is phosphorylated on an N-terminal serine residue ( s ) within the DELLA/TVHYNP and polyS/T/V domain .
However , gibberellin-induced phosphorylation in these regions was not observed in the gid2 mutant following the constitutive expression of SLR1 under the control of the rice actin1 promoter .
Treatment with gibberellin induced both the phosphorylated and non-phosphorylated forms of SLR1 with similar induction kinetics in gid2 mutant cells .
Both the phosphorylated and non-phosphorylated SLR1 proteins were degraded by gibberellin treatment with a similar half-life in the rice callus cells , and both proteins interacted with recombinant glutathione S-transferase ( GST ) -GID2 .
These results demonstrate that the phosphorylation of SLR1 is independent of its degradation and is dispensable for the interaction of SLR1 with the GID2/F-box protein . | Matching Sentences:
[ Sen. 3, subscore: 2.00 ]: In addition , the gibberellin-dependent increase of phosphorylated SLR1 in the loss-of-function gid2 mutant suggests that the SCF ( GID2 ) -mediated degradation of SLR1 might be initiated by gibberellin-dependent phosphorylation .
[ Sen. 4, subscore: 2.00 ]: To confirm the role of phosphorylation of SLR1 in its gibberellin-dependent degradation , we revealed that SLR1 is phosphorylated on an N-terminal serine residue ( s ) within the DELLA/TVHYNP and polyS/T/V domain .
[ Sen. 8, subscore: 2.00 ]: These results demonstrate that the phosphorylation of SLR1 is independent of its degradation and is dispensable for the interaction of SLR1 with the GID2/F-box protein .
[ Sen. 2, subscore: 1.00 ]: Our previous studies have indicated that gibberellin signaling is derepressed by SCF ( GID2 ) -mediated proteolysis of the DELLA protein , SLENDER RICE1 ( SLR1 ) , in rice .
[ Sen. 5, subscore: 1.00 ]: However , gibberellin-induced phosphorylation in these regions was not observed in the gid2 mutant following the constitutive expression of SLR1 under the control of the rice actin1 promoter .
[ Sen. 6, subscore: 1.00 ]: Treatment with gibberellin induced both the phosphorylated and non-phosphorylated forms of SLR1 with similar induction kinetics in gid2 mutant cells .
[ Sen. 7, subscore: 1.00 ]: Both the phosphorylated and non-phosphorylated SLR1 proteins were degraded by gibberellin treatment with a similar half-life in the rice callus cells , and both proteins interacted with recombinant glutathione S-transferase ( GST ) -GID2 .
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Score: 9.00 |
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| Title: Release of the repressive activity of rice DELLA protein SLR1 by gibberellin does not require SLR1 degradation in the gid2 mutant .
| | Author: Ueguchi-Tanaka M Hirano K Hasegawa Y Kitano H Matsuoka M | | Journal: Plant Cell Citation: V : 20 P : 2437-46 Year: 2008 Type: In-Process | | Literature: oryza Field: abstract Doc ID: pub18827181 Accession (PMID): 18827181 | | Abstract: The rice ( Oryza sativa ) DELLA protein SLR1 acts as a repressor of gibberellin ( GA ) signaling .
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 .
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 .
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 .
Based on these observations , we propose a model for the release of GA suppression that does not require DELLA protein degradation .
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[ Sen. 3, subscore: 2.00 ]: 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 .
[ Sen. 1, subscore: 1.00 ]: The rice ( Oryza sativa ) DELLA protein SLR1 acts as a repressor of gibberellin ( GA ) signaling .
[ Sen. 2, subscore: 1.00 ]: 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 .
[ Sen. 4, subscore: 1.00 ]: 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 .
[ Sen. 5, subscore: 1.00 ]: 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 .
[ Sen. 6, subscore: 1.00 ]: Conversely , overproduction of GID1 or treatment with GA ( 3 ) increased the SLR1 level in gid2 and reduced dwarfism .
[ Sen. 7, subscore: 1.00 ]: 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 .
[ Sen. 8, subscore: 1.00 ]: 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 .
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