Os03g0707600 - Revision history

Longyihu: /* References */

2014-05-27T16:43:13Z

‎References

Longyihu: /* References */

2014-05-27T16:40:01Z

‎References

Longyihu: /* Knowledge Extension */

2014-05-27T16:37:18Z

‎Knowledge Extension

Longyihu: /* Knowledge Extension */

2014-05-27T16:37:04Z

‎Knowledge Extension

Longyihu: /* Knowledge Extension */

2014-05-27T16:36:43Z

‎Knowledge Extension

Longyihu: /* Mutation */

2014-05-27T16:33:56Z

‎Mutation

Longyihu: /* Mutation */

2014-05-27T16:33:01Z

‎Mutation

Longyihu: /* Mutation */

2014-05-27T16:32:14Z

‎Mutation

Longyihu: /* Function */

2014-05-27T16:26:17Z

‎Function

Longyihu: /* Function */

2014-05-27T16:25:35Z

‎Function

@@ Line 60: / Line 60: @@
 <ref name="ref11">Harberd NP, Belfield E, Yasumura Y, The angiosperm gibberellin-GID1-DELLA growth regulatory mechanism: how an "inhibitor of an inhibitor" enables flexible response to fluctuating environments. The Plant cell, 2009, 21:1328-1339</ref>
-==Structured Information==
+== Structured Information ==
 {{JaponicaGene|
 GeneName = Os03g0707600|

@@ Line 58: / Line 58: @@
 <ref name="ref9">Hirano K, Kouketu E, Katoh H, et al. The suppressive function of the rice DELLA protein SLR1 is dependent on its transcriptional activation activity[J]. The Plant Journal, 2012, 71(3): 443-453.</ref>
 <ref name="ref10">Ueguchi-Tanaka M, Nakajima M, Katoh E,  Yamaguchi I, Matsuoka M, et al. Molecular interactions of a soluble gibberellin receptor, GID1, with a rice DELLA protein, SLR1, and gibberellin. The Plant cell,2007, 19:2140-2155</ref>
 ==Structured Information==

@@ Line 34: / Line 34: @@
 === Knowledge Extension ===
-[[File:4.jpg|right|thumb|200px|''Molecular model for the suppressive function of SLR1 and inhibition of the suppressive function of SLR1 by GID1 during plant growth (from reference <ref name="ref9" />).'']]
+[[File:4.jpg|right|thumb|200px|''Molecular model for the suppressive function of SLR1 and inhibition of the suppressive function of SLR1 by GID1 during plant growth (from reference <ref name="ref11" />).'']]
 [[File:5.jpg|right|thumb|200px|''The GA signaling pathway (from reference <ref name="ref9" />).'']]
 When GA4 binds to GID1 (a soluble GA receptor), SLR1 interacts with the GID1-GA complex at its N-terminal region, including the DELLA and TVHYNP domains. The stabilized complex of GA, GID1, and SLR1 may be targeted by GID2, an F-box protein, leading to its degradation by 26S proteasomes through ubiquitination of the SCF GID2 complex, and then the GA response is active through repression of the repressor SLR1<ref name="ref10" />. The stable interaction of GID1-SLR1 through the GRAS domain is essential for the recognition of SLR1 by GID2. 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 <ref name="ref7" />. The N-terminal region of SLR1 has two roles in GA signaling: interaction with GID1 and transactivation activity, and the suppressive function of the rice DELLA protein SLR1 is dependent on its transcriptional activation activity <ref name="ref9" />. However, in the gid2 mutant, release of the repressive activity of rice DELLA protein SLR1 by GA does not require SLR1 degradation <ref name="ref5" />. SLR1 mediates the interaction between GA and ABA by upregulation of endogenous ABA level and downregulation of endogenous of GA level <ref name="ref4" />.

@@ Line 34: / Line 34: @@
 === Knowledge Extension ===
-[[File:4.jpg|right|thumb|150px|''Molecular model for the suppressive function of SLR1 and inhibition of the suppressive function of SLR1 by GID1 during plant growth (from reference <ref name="ref9" />).'']]
+[[File:4.jpg|right|thumb|200px|''Molecular model for the suppressive function of SLR1 and inhibition of the suppressive function of SLR1 by GID1 during plant growth (from reference <ref name="ref9" />).'']]
 [[File:5.jpg|right|thumb|200px|''The GA signaling pathway (from reference <ref name="ref9" />).'']]
 When GA4 binds to GID1 (a soluble GA receptor), SLR1 interacts with the GID1-GA complex at its N-terminal region, including the DELLA and TVHYNP domains. The stabilized complex of GA, GID1, and SLR1 may be targeted by GID2, an F-box protein, leading to its degradation by 26S proteasomes through ubiquitination of the SCF GID2 complex, and then the GA response is active through repression of the repressor SLR1<ref name="ref10" />. The stable interaction of GID1-SLR1 through the GRAS domain is essential for the recognition of SLR1 by GID2. 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 <ref name="ref7" />. The N-terminal region of SLR1 has two roles in GA signaling: interaction with GID1 and transactivation activity, and the suppressive function of the rice DELLA protein SLR1 is dependent on its transcriptional activation activity <ref name="ref9" />. However, in the gid2 mutant, release of the repressive activity of rice DELLA protein SLR1 by GA does not require SLR1 degradation <ref name="ref5" />. SLR1 mediates the interaction between GA and ABA by upregulation of endogenous ABA level and downregulation of endogenous of GA level <ref name="ref4" />.

← Older revision		Revision as of 16:36, 27 May 2014
Line 34:		Line 34:

	=== Knowledge Extension ===		=== Knowledge Extension ===
		+	[[File:4.jpg\|right\|thumb\|150px\|''Molecular model for the suppressive function of SLR1 and inhibition of the suppressive function of SLR1 by GID1 during plant growth (from reference <ref name="ref9" />).'']]
		+	[[File:5.jpg\|right\|thumb\|200px\|''The GA signaling pathway (from reference <ref name="ref9" />).'']]
	When GA4 binds to GID1 (a soluble GA receptor), SLR1 interacts with the GID1-GA complex at its N-terminal region, including the DELLA and TVHYNP domains. The stabilized complex of GA, GID1, and SLR1 may be targeted by GID2, an F-box protein, leading to its degradation by 26S proteasomes through ubiquitination of the SCF GID2 complex, and then the GA response is active through repression of the repressor SLR1<ref name="ref10" />. The stable interaction of GID1-SLR1 through the GRAS domain is essential for the recognition of SLR1 by GID2. 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 <ref name="ref7" />. The N-terminal region of SLR1 has two roles in GA signaling: interaction with GID1 and transactivation activity, and the suppressive function of the rice DELLA protein SLR1 is dependent on its transcriptional activation activity <ref name="ref9" />. However, in the gid2 mutant, release of the repressive activity of rice DELLA protein SLR1 by GA does not require SLR1 degradation <ref name="ref5" />. SLR1 mediates the interaction between GA and ABA by upregulation of endogenous ABA level and downregulation of endogenous of GA level <ref name="ref4" />.		When GA4 binds to GID1 (a soluble GA receptor), SLR1 interacts with the GID1-GA complex at its N-terminal region, including the DELLA and TVHYNP domains. The stabilized complex of GA, GID1, and SLR1 may be targeted by GID2, an F-box protein, leading to its degradation by 26S proteasomes through ubiquitination of the SCF GID2 complex, and then the GA response is active through repression of the repressor SLR1<ref name="ref10" />. The stable interaction of GID1-SLR1 through the GRAS domain is essential for the recognition of SLR1 by GID2. 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 <ref name="ref7" />. The N-terminal region of SLR1 has two roles in GA signaling: interaction with GID1 and transactivation activity, and the suppressive function of the rice DELLA protein SLR1 is dependent on its transcriptional activation activity <ref name="ref9" />. However, in the gid2 mutant, release of the repressive activity of rice DELLA protein SLR1 by GA does not require SLR1 degradation <ref name="ref5" />. SLR1 mediates the interaction between GA and ABA by upregulation of endogenous ABA level and downregulation of endogenous of GA level <ref name="ref4" />.

@@ Line 9: / Line 9: @@
 === Mutation ===
 [[File:3.jpg|right|thumb|200px|''the ''slr1-1'' mutant shows slender phenotype (from reference <ref name="ref2" />).'']]
-[[File:2.jpg|right|thumb|200px|''''Slr1-d1, Slr1-d2, and Slr1-d3'' show semidwarf phenotype (from reference <ref name="ref2" />).'']]
+[[File:2.jpg|right|thumb|200px|''the ''Slr1-d1'', ''Slr1-d2'', and ''Slr1-d3'' mutants show semidwarf phenotype (from reference <ref name="ref2" />).'']]
 Slr1-1 mutant which shows a slender phenotype is caused by a single recessive mutation and results in a constitutive GA response phenotype. It has a 17–amino acid deletion affecting the DELLA region, which results in a loss-of-function mutation of the SLR1 gene, which is an ortholog of RHT-1Da in wheat, D8 in maize, and GAI and RGA in Arabidopsis <ref name="ref2" />. The slr1-1allele contained one base deletion at Leu289, a putative NLS region, which alters the N-terminal region of the protein that it encodes. The other three alleles (slr1-2, slr1-3 and slr1-4) contained premature stop codons <ref name="ref2" />.

← Older revision		Revision as of 16:32, 27 May 2014
Line 8:		Line 8:

	=== Mutation ===		=== Mutation ===
		+	[[File:3.jpg\|right\|thumb\|200px\|''the ''slr1-1'' mutant shows slender phenotype (from reference <ref name="ref2" />).'']]
		+	[[File:2.jpg\|right\|thumb\|200px\|''''Slr1-d1, Slr1-d2, and Slr1-d3''show semidwarf phenotype (from reference <ref name="ref2" />).'']]
	Slr1-1 mutant which shows a slender phenotype is caused by a single recessive mutation and results in a constitutive GA response phenotype. It has a 17–amino acid deletion affecting the DELLA region, which results in a loss-of-function mutation of the SLR1 gene, which is an ortholog of RHT-1Da in wheat, D8 in maize, and GAI and RGA in Arabidopsis <ref name="ref2" />. The slr1-1allele contained one base deletion at Leu289, a putative NLS region, which alters the N-terminal region of the protein that it encodes. The other three alleles (slr1-2, slr1-3 and slr1-4) contained premature stop codons <ref name="ref2" />.		Slr1-1 mutant which shows a slender phenotype is caused by a single recessive mutation and results in a constitutive GA response phenotype. It has a 17–amino acid deletion affecting the DELLA region, which results in a loss-of-function mutation of the SLR1 gene, which is an ortholog of RHT-1Da in wheat, D8 in maize, and GAI and RGA in Arabidopsis <ref name="ref2" />. The slr1-1allele contained one base deletion at Leu289, a putative NLS region, which alters the N-terminal region of the protein that it encodes. The other three alleles (slr1-2, slr1-3 and slr1-4) contained premature stop codons <ref name="ref2" />.

@@ Line 4: / Line 4: @@
 ==Annotated Information==
 ===Function===
-[[File:1.jpg|right|thumb|300px|''The slr1 protein Domain (from reference <ref name="ref3" />).'']]
+[[File:1.jpg|right|thumb|300px|''The slr1 protein sturcture domain (from reference <ref name="ref3" />).'']]
 OsGAI, also known as slender rice 1(SLR1), is first identified as a homolog of the GAI gene of Arabidopsis <ref name="ref1" />. It encodes a rice DELLA protein of 625 amino acids, which is characterized as a member of the GRAS family. Sequences analyses reveal that SLR1 contains a valine (polyS/T/V), a DELLA box, a TVHYNP region, a nuclear localization signal (NLS), a leucine heptad repeat (LZ) and the VHIID motif in N-terminal and the PFYRE motif and the SAW motif in C-terminal <ref name="ref3" />. In addition, function domain analyses reveal that the SLR1 protein can be divided into four parts: 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, a GA signal perception domain located at the N terminus <ref name="ref3" />. Gibberellin (GA), a key phytohormone, controls many crucial aspects during the whole life cycle of plants, including germination, stem elongation, flower development and stress response. The study of mutant indicates that SLR1 is a negative regulator in GA signaling pathway, and overexpressing SLR1 gene in transgenic rice plants cause dwarf phenotype <ref name="ref3" />. DELLA protein SLR1 represses the GA-response gene expression by direct binding to transcription factor of target gene. Application of exogenous GA causes disappearance of SLR1-GFP in nuclei <ref name="ref3" />.