Os02g0580300 - Revision history

Xysj2017 at 02:35, 14 February 2017

2017-02-14T02:35:04Z

Xysj2017: /* References */

2017-02-14T02:34:35Z

‎References

Xysj2017 at 02:34, 14 February 2017

2017-02-14T02:34:10Z

Xysj2012: /* Structured Information */

2015-05-14T05:44:13Z

‎Structured Information

Jiangboling: /* Function */

2014-05-24T06:26:14Z

‎Function

Jiangboling: /* Function */

2014-05-24T06:22:03Z

‎Function

Jiangboling: /* Annotated Information */

2014-05-22T08:11:23Z

‎Annotated Information

Jiangboling: /* Annotated Information */

2014-05-22T08:09:20Z

‎Annotated Information

Jiangboling: /* Annotated Information */

2014-05-22T07:44:19Z

‎Annotated Information

Jiangboling: /* Expression */

2014-05-22T07:23:13Z

‎Expression

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 ===Evolution===
-The F-box domain in GID2 is well conserved in other F-box proteins, with the greatest similarity to Arabidopsis SLY1, which is a positive regulator of GA signaling(Fig. 8)[[File:8.png|thumb|right|Fig.8. Alignment of the F-box motif of GID2 with other F-box proteins(from reference<ref name="ref1" />.)]].<ref name="ref1" />.F-box proteins occur widely throughout the eukaryote kingdom, in organisms ranging from yeast to humans, and they function as receptors that recuit proteins as substrates for ubiquitin-mediated degradation in the 26S proteasome<ref name="ref3" />.
+The F-box domain in GID2 is well conserved in other F-box proteins, with the greatest similarity to Arabidopsis SLY1, which is a positive regulator of GA signaling(Fig. 8).<ref name="ref1" />.F-box proteins occur widely throughout the eukaryote kingdom, in organisms ranging from yeast to humans, and they function as receptors that recuit proteins as substrates for ubiquitin-mediated degradation in the 26S proteasome<ref name="ref3" />.
 The SCF-mediated signaling pathway is well conserved in yeast, mammals and higher plants. GA-dependent phosphorylation of SLR1 triggers the ubiquitin-mediated degradation in a manner similar to the SCF-mediated in yeast and animals<ref name="ref1" />.

← Older revision		Revision as of 02:34, 14 February 2017
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	<ref name="ref4"> Ko Hirano, Kenji Asano, Hiroyuki Tsuji, Mayuko Kawamura, Hitoshi Mori, Hidemi Kitano, Miyako Ueguchi-Tanaka, and Makoto Matsuoka. Characterization of the Molecular Mechanism Underlying Gibberellin Perception Complex Formation in Rice. The Plant Cell, 2010( 22): 2680–2696.</ref>		<ref name="ref4"> Ko Hirano, Kenji Asano, Hiroyuki Tsuji, Mayuko Kawamura, Hitoshi Mori, Hidemi Kitano, Miyako Ueguchi-Tanaka, and Makoto Matsuoka. Characterization of the Molecular Mechanism Underlying Gibberellin Perception Complex Formation in Rice. The Plant Cell, 2010( 22): 2680–2696.</ref>
−
−	~~<ref name="ref5"> Bolle, C. (2004). The role of GRAS proteins in plant signal transduction and development. Planta 218: 683–692.</ref>~~

	</references>		</references>

@@ Line 17: / Line 17: @@
 The ''gid2'' is a rice GA-insensitive dwarf mutant. It is caused by the loss function of a putative F-box protein.
 The ''gid2'' mutant shows a severe dwarf phenotype with wide leaf blades and dark green leaves(Fig.5)[[File:5.png|thumb|right|Fig.5. Phenotype of the ''gid2'' mutant(from reference<ref name="ref1" />.)]], fetures typical of GA-related mutants such as d1 and d18. The ''gid2-1/slr-1'' double mutants show a slender phenotype identical to that of the ''slr-1'' single mutants, indicating that GID2 functions upstream of SLR1<ref name="ref1" />.
-The ''gid2'' mutants are dwarfed because they accumulate SLR1.The ''gid2'' mutants exhibit reduced GA responses and don’t resume normal growth when treated with GA<ref name="ref2" />. In ''gid2'', a repressor for GA signaling, SLR1, is highly accumulated in a phosphorylated form and GA increases its concentration in the wild type(Fig. 6)[[File:6.png|thumb|right|Fig.6. Accumulation of the phosphorylated SLR1 protein in ''gid2''(from reference<ref name="ref1" />.)]].Dgradation of SLR1 protein does not occur in ''gid2'' mutants(Fig. 7)[[File:7.jpg|thumb|right|Fig.7.(from reference<ref name="ref3" />.)]].. The accumulated SLR1 is located in the nuclei, as it is in the wild type<ref name="ref1" />.
+The ''gid2'' mutants are dwarfed because they accumulate SLR1.The ''gid2'' mutants exhibit reduced GA responses and don’t resume normal growth when treated with GA<ref name="ref2" />. In ''gid2'', a repressor for GA signaling, SLR1, is highly accumulated in a phosphorylated form and GA increases its concentration in the wild type(Fig. 6)[[File:6.png|thumb|right|Fig.6. Accumulation of the phosphorylated SLR1 protein in ''gid2''(from reference<ref name="ref1" />.)]].Dgradation of SLR1 protein does not occur in ''gid2'' mutants(Fig. 7)
 ===Evolution===
@@ Line 30: / Line 30: @@
 '''IdentificationofSLR1RegionsImportant for Interaction with GID1 and GID2'''
-The GRAS domain has been divided into several subdomains: LHRI, VHIID, LHRII, PFYRE, and SAW(Fig. 9)[[File:9.png|thumb|right|Fig.9. Schematic structure of SLR1(from reference<ref name="ref4" />.)]].<ref name="ref5" />. In DELLA proteins, the DELLA/TVHYNP motif and the GRAS domain are connected by the poly S/T/V domain, a domain that shows large sequence variation among DELLA proteins. Poly S/T/V and LHRI are not important for the interaction with GID1 or GID2. VHIID is important for the interaction with GID2. LHRII is also important for interaction with GID2 and may be partially involved in the stable interaction with GID1. In the case of the PFYRE and SAW subdomains, the overall trend of the mutant proteins is apparently different from that of the previous four subdomains, and there are two valleys of interaction with GID1 in each one. Exchanges of DRF490-2AAA or HYY497-9AAA in the PFYRE subdomain dramatically reduced the interaction with GID1 and nearly eliminated GID2 interaction. In the SAW subdomain, G576V abolished interaction with both GID1 and GID2, as previously observed<ref name="ref4" />.
+The GRAS domain has been divided into several subdomains: LHRI, VHIID, LHRII, PFYRE, and SAW(Fig. 9) In DELLA proteins, the DELLA/TVHYNP motif and the GRAS domain are connected by the poly S/T/V domain, a domain that shows large sequence variation among DELLA proteins. Poly S/T/V and LHRI are not important for the interaction with GID1 or GID2. VHIID is important for the interaction with GID2. LHRII is also important for interaction with GID2 and may be partially involved in the stable interaction with GID1. In the case of the PFYRE and SAW subdomains, the overall trend of the mutant proteins is apparently different from that of the previous four subdomains, and there are two valleys of interaction with GID1 in each one. Exchanges of DRF490-2AAA or HYY497-9AAA in the PFYRE subdomain dramatically reduced the interaction with GID1 and nearly eliminated GID2 interaction. In the SAW subdomain, G576V abolished interaction with both GID1 and GID2, as previously observed<ref name="ref4" />.
 '''Domain Analysis of GA Signaling Components and a Model of GID1-SLR1-GID2 Complex Formation'''
-In GID2, the GGF and LSL domains are necessary for the interaction with SLR1, GID1 regions other than those involved in the GID1-SLR1 interaction are not necessary for the SLR1-GID2 interaction. In SLR1, the poly S/T/V and LHRI subdomains might not be involved in the interaction with either GID1 or GID2. VHIID and LHRII seem to be preferentially involved in the interaction with GID2 and might be the direct GID2 binding site. The C-terminal region of the VHIID subdomain (LQ361-2) is also involved in the interaction with GID1(Fig. 10)[[File:10.png|thumb|right|Fig.10. Molecular model for the Formation of the GID1-SLR1-GID2 Complex(from reference<ref name="ref4" />.)]]<ref name="ref4" />.
+In GID2, the GGF and LSL domains are necessary for the interaction with SLR1, GID1 regions other than those involved in the GID1-SLR1 interaction are not necessary for the SLR1-GID2 interaction. In SLR1, the poly S/T/V and LHRI subdomains might not be involved in the interaction with either GID1 or GID2. VHIID and LHRII seem to be preferentially involved in the interaction with GID2 and might be the direct GID2 binding site. The C-terminal region of the VHIID subdomain (LQ361-2) is also involved in the interaction with GID1(Fig. 10)<ref name="ref4" />.

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 ==Structured Information==
 [[Category:Genes]]
 [[Category:Japonica mRNA]]

@@ Line 4: / Line 4: @@
 ===Function===
 The ''GID2'' gene encoded a 639-base-pair open reading frame capable of producing a
-polypeptide of 212 amino acid residues. The deduced amino acid sequence of GID2 contained an F-box domain(Fig. 1)[[File:1.png|thumb|right|Fig.1. Sequence analyses and molecular characterization of ''GID2''(from reference<ref name="ref1" />.)]]<ref name="ref1" />.F-box domains are found in specific components of the multisubunit SCF E3 ubiquitin ligase complex.<ref name="ref2" />The F-box protein in the SCF complex functions as a receptor that selectively recuits target proteins into the complex to degrade those proteins through ubiquitination<ref name="ref1" />.
+polypeptide of 212 amino acid residues. The deduced amino acid sequence of GID2 contained an F-box domain(Fig. 1)[[File:1.1.png|thumb|right|Fig.1. Sequence analyses and molecular characterization of ''GID2''(from reference<ref name="ref1" />.)]]<ref name="ref1" />.F-box domains are found in specific components of the multisubunit SCF E3 ubiquitin ligase complex.<ref name="ref2" />The F-box protein in the SCF complex functions as a receptor that selectively recuits target proteins into the complex to degrade those proteins through ubiquitination<ref name="ref1" />.
 GID2 influences the rice height through regulating GA signaling. GA are essential regulators of diverse growth and developmental process in plants. A GA signal promotes the degradation of SLR1 by the post-translational modification to be targeted by GID2<ref name="ref3" />.
 GID2 is a component of the SCF complex through an inieraction with a rice ASK1 homolog,OsSkp15(Fig. 2)[[File:2.png|thumb|right|Fig.2. GID2 is a component of the SCF complex(from reference<ref name="ref3" />.)]].GID2 is a positive regulator of GA signaling and that regulated degradation of SLR1 is initiated through GA-dependent phosphorylation and finalized by an SCF-GID2 proteasome pathway.The SLR1 protein functions as a repressor of GA signaling in rice and its degradation is essential for downstream action of GA. The SCF-GID2 complex mediate the ubiquition/26S proteasome pathway(Fig. 3)[[File:3.png|thumb|right|Fig.3. GID2 in nuclei interacts with the phosphorylated form of SLR1(from reference<ref name="ref3" />.)]]<<ref name="ref2" /><ref name="ref3" />.

@@ Line 23: / Line 23: @@
 The SCF-mediated signaling pathway is well conserved in yeast, mammals and higher plants. GA-dependent phosphorylation of SLR1 triggers the ubiquitin-mediated degradation in a manner similar to the SCF-mediated in yeast and animals<ref name="ref1" />.
-===Knowledge Extention===
+===Knowledge Extension===
 The interaction between GIBBERELLIN INSENSITIVE DWARF1 (GID1) and the N-terminal DELLA/TVHYNP motif of SLR1 triggers F-box protein GID2-mediated SLR1 degradation.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.
 In the absence of GA, DELLA represses GA action. When GA is present, the GA-bound GID1 receptor interacts with the DELLA/TVHYNP motif of DELLA protein. This interaction triggers DELLA protein degradation through the SCF-GID2/SLY1 proteasome pathway, and GA action occurs

@@ Line 4: / Line 4: @@
 ===Function===
 The ''GID2'' gene encoded a 639-base-pair open reading frame capable of producing a
-polypeptide of 212 amino acid residues. The deduced amino acid sequence of GID2 contained an F-box domain(Fig. 1)[[File:1.png|thumb|right(from reference<ref name="ref1" />.)]]<ref name="ref1" />.F-box domains are found in specific components of the multisubunit SCF E3 ubiquitin ligase complex.<ref name="ref2" />The F-box protein in the SCF complex functions as a receptor that selectively recuits target proteins into the complex to degrade those proteins through ubiquitination<ref name="ref1" />.
+polypeptide of 212 amino acid residues. The deduced amino acid sequence of GID2 contained an F-box domain(Fig. 1)[[File:1.png|thumb|right|Fig.2. Sequence analyses and molecular characterization of ''GID2''(from reference<ref name="ref1" />.)]]<ref name="ref1" />.F-box domains are found in specific components of the multisubunit SCF E3 ubiquitin ligase complex.<ref name="ref2" />The F-box protein in the SCF complex functions as a receptor that selectively recuits target proteins into the complex to degrade those proteins through ubiquitination<ref name="ref1" />.
 GID2 influences the rice height through regulating GA signaling. GA are essential regulators of diverse growth and developmental process in plants. A GA signal promotes the degradation of SLR1 by the post-translational modification to be targeted by GID2<ref name="ref3" />.
-GID2 is a component of the SCF complex through an inieraction with a rice ASK1 homolog,OsSkp15(Fig. 2)[[File:2.png|thumb|right(from reference<ref name="ref3" />.)]].GID2 is a positive regulator of GA signaling and that regulated degradation of SLR1 is initiated through GA-dependent phosphorylation and finalized by an SCF-GID2 proteasome pathway.The SLR1 protein functions as a repressor of GA signaling in rice and its degradation is essential for downstream action of GA. The SCF-GID2 complex mediate the ubiquition/26S proteasome pathway(Fig. 3)[[File:3.png|thumb|right(from reference<ref name="ref3" />.)]]<<ref name="ref2" /><ref name="ref3" />.
+GID2 is a component of the SCF complex through an inieraction with a rice ASK1 homolog,OsSkp15(Fig. 2)[[File:2.png|thumb|right|Fig.4. GID2 is a component of the SCF complex(from reference<ref name="ref3" />.)]].GID2 is a positive regulator of GA signaling and that regulated degradation of SLR1 is initiated through GA-dependent phosphorylation and finalized by an SCF-GID2 proteasome pathway.The SLR1 protein functions as a repressor of GA signaling in rice and its degradation is essential for downstream action of GA. The SCF-GID2 complex mediate the ubiquition/26S proteasome pathway(Fig. 3)[[File:3.png|thumb|right|Fig.3. GID2 in nuclei interacts with the phosphorylated form of SLR1(from reference<ref name="ref3" />.)]]<<ref name="ref2" /><ref name="ref3" />.
 ===Domain analysis of GID2===
@@ Line 12: / Line 12: @@
 ===Expression===
-The ''GID2'' gene is expressed at different levels in all organs, preferentially expressed in unopened flowers, shoot apices, and elongation stem, and at lower levels in the leaf blades, leaf sheaths, roots, and rachis. Expression of ''GID2'' preferentially occurs in rice organs actively synthesizing GA(Fig. 4)[[File:4.jpg|200px|thumb|right(from reference<ref name="ref3" />.)]]<ref name="ref3" />.
+The ''GID2'' gene is expressed at different levels in all organs, preferentially expressed in unopened flowers, shoot apices, and elongation stem, and at lower levels in the leaf blades, leaf sheaths, roots, and rachis. Expression of ''GID2'' preferentially occurs in rice organs actively synthesizing GA(Fig. 4)[[File:4.jpg|thumb|right|Fig.4. Expression patterns of the ''GID2'' gene in various plant organs(from reference<ref name="ref3" />.)]]<ref name="ref3" />.
 ===Mutant===
 The ''gid2'' is a rice GA-insensitive dwarf mutant. It is caused by the loss function of a putative F-box protein.
-The ''gid2'' mutant shows a severe dwarf phenotype with wide leaf blades and dark green leaves, fetures typical of GA-related mutants such as d1 and d18. The ''gid2-1/slr-1'' double mutants show a slender phenotype identical to that of the ''slr-1'' single mutants, indicating that GID2 functions upstream of SLR1<ref name="ref1" />.
+The ''gid2'' mutant shows a severe dwarf phenotype with wide leaf blades and dark green leaves(Fig.5)[[File:5.png|thumb|right|Fig.5. Phenotype of the ''gid2'' mutant(from reference<ref name="ref1" />.)]], fetures typical of GA-related mutants such as d1 and d18. The ''gid2-1/slr-1'' double mutants show a slender phenotype identical to that of the ''slr-1'' single mutants, indicating that GID2 functions upstream of SLR1<ref name="ref1" />.
-The ''gid2'' mutants are dwarfed because they accumulate SLR1.The ''gid2'' mutants exhibit reduced GA responses and don’t resume normal growth when treated with GA<ref name="ref2" />. In ''gid2'', a repressor for GA signaling, SLR1, is highly accumulated in a phosphorylated form and GA increases its concentration in the wild type.Dgradation of SLR1 protein does not occur in ''gid2'' mutants. The accumulated SLR1 is located in the nuclei, as it is in the wild type<ref name="ref1" />.
+The ''gid2'' mutants are dwarfed because they accumulate SLR1.The ''gid2'' mutants exhibit reduced GA responses and don’t resume normal growth when treated with GA<ref name="ref2" />. In ''gid2'', a repressor for GA signaling, SLR1, is highly accumulated in a phosphorylated form and GA increases its concentration in the wild type(Fig. 6)[[File:6.png|thumb|right|Fig.6. Accumulation of the phosphorylated SLR1 protein in ''gid2''(from reference<ref name="ref1" />.)]].Dgradation of SLR1 protein does not occur in ''gid2'' mutants(Fig. 7)[[File:7.jpg|thumb|right|Fig.7.(from reference<ref name="ref3" />.)]].. The accumulated SLR1 is located in the nuclei, as it is in the wild type<ref name="ref1" />.
 ===Evolution===
-The F-box domain in GID2 is well conserved in other F-box proteins, with the greatest similarity to Arabidopsis SLY1, which is a positive regulator of GA signaling<ref name="ref1" />.F-box proteins occur widely throughout the eukaryote kingdom, in organisms ranging from yeast to humans, and they function as receptors that recuit proteins as substrates for ubiquitin-mediated degradation in the 26S proteasome<ref name="ref3" />.
+The F-box domain in GID2 is well conserved in other F-box proteins, with the greatest similarity to Arabidopsis SLY1, which is a positive regulator of GA signaling(Fig. 8)[[File:8.png|thumb|right|Fig.8. Alignment of the F-box motif of GID2 with other F-box proteins(from reference<ref name="ref1" />.)]].<ref name="ref1" />.F-box proteins occur widely throughout the eukaryote kingdom, in organisms ranging from yeast to humans, and they function as receptors that recuit proteins as substrates for ubiquitin-mediated degradation in the 26S proteasome<ref name="ref3" />.
 The SCF-mediated signaling pathway is well conserved in yeast, mammals and higher plants. GA-dependent phosphorylation of SLR1 triggers the ubiquitin-mediated degradation in a manner similar to the SCF-mediated in yeast and animals<ref name="ref1" />.