Os02g0656600 - Revision history

Zhennan: /* References */

2017-03-23T07:41:14Z

‎References

Zhennan at 07:40, 23 March 2017

2017-03-23T07:40:59Z

Xysj2012: Blanked the page

2016-12-30T05:54:02Z

Blanked the page

Xysj2012 at 05:50, 14 May 2015

2015-05-14T05:50:39Z

Xiaopeiwu0509: /* References */

2014-05-28T01:46:57Z

‎References

Xiaopeiwu0509: /* Mutations */

2014-05-28T01:34:19Z

‎Mutations

Xiaopeiwu0509: /* Mutations */

2014-05-28T01:33:05Z

‎Mutations

Xiaopeiwu0509: /* Localization */

2014-05-27T14:59:26Z

‎Localization

Xiaopeiwu0509: /* Mutations */

2014-05-27T14:43:12Z

‎Mutations

Xiaopeiwu0509: /* Function */

2014-05-27T14:39:14Z

‎Function

← Older revision		Revision as of 07:41, 23 March 2017
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	</ref>		</ref>
	</references>		</references>
		+
		+	<br>

← Older revision	Revision as of 07:40, 23 March 2017
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	+	The rice '''''Os02g0656600''''' was reported as '''''OsERF#032''''' in 2006 <ref name="ref1" /> by researchers from Japan.

	+	==Annotated Information==
	+	===Gene Symbol===
	+	*'''''Os02g0656600''''' '''''<=>''''' '''''OsERF#032'''''
	+
	+	===Function===
	+	* Genes in the ERF family encode transcriptional regulators with a variety of functions involved in the developmental and physiological processes in plants.
	+	* It has been demonstrated that the AP2/ERF proteins have important functions in the transcriptional regulation of a variety of biological processes related to growth and development, as well as various responses to environmental stimuli.
	+	* Genes in the AP2 family have been shown to participate in the regulation of developmental processes, e.g. flower development (Elliott et al., 1996), spikelet meristem determinacy (Chuck et al., 1998), leaf epidermal cell identity (Moose and Sisco, 1996), and embryo development (Boutilier et al., 2002).<ref name="ref2" />
	+
	+	===Evolution===
	+	* The ERF family is a large gene family of transcription factors and is part of the AP2/ERF superfamily, which also contains the AP2 and RAV families
	+	* The AP2/ERF superfamily is defined by the AP2/ERF domain, which consists of about 60 to 70 amino acids and is involved in DNA binding.
	+	* The AP2 family proteins contain two repeated AP2/ERF domains, the ERF family proteins contain a single AP2/ERF domain, and the RAV family proteins contain a B3 domain, which is a DNA-binding domain conserved in other plant-specific transcription factors, including VP1/ABI3, in addition to the single AP2/ERF domain.
	+	* The expansion of the ERF family in plants might have been due to chromosomal/segmental duplication and tandem duplication, as well as more ancient transposition and homing.
	+	* Since rice is a cultivated species, selection either during domestication from its wild ancestor or during agricultural improvement in the subsequent time may also have been important for the evolution of rice ERF family.<ref name="ref3" />
	+
	+	You can also add sub-section(s) at will.
	+
	+	==Labs working on this gene==
	+	* Molecular and Cellular Breeding Research Group, Institute for Biological Resources and Functions, National Institute of Advanced Industrial Science and Technology, Tsukuba, Ibaraki 305–8566, Japan (T.N., K.S., H.S.);
	+	* Graduate School of Life and Environmental Sciences, University of Tsukuba, Tsukuba, Ibaraki 305–8672, Japan (T.N., T.F.)
	+
	+
	+	==References==
	+	<references>
	+	* <ref name="ref1">
	+	Nakano T, Suzuki K, Fujimura T, Shinshi H. Genome-wide analysis of the ERF
	+	gene family in Arabidopsis and rice. Plant Physiol. 2006 Feb;140(2):411-32.
	+	PubMed PMID: 16407444; PubMed Central PMCID: PMC1361313.
	+	</ref>
	+	* <ref name="ref2">
	+	Chuck G, Muszynski M, Kellogg E, Hake S, Schmidt RJ. The control of spikelet
	+	meristem identity by the branched silkless1 gene in maize. Science. 2002 Nov
	+	8;298(5596):1238-41. PubMed PMID: 12424380.
	+	</ref>
	+	* <ref name="ref3">
	+	Riechmann JL, Meyerowitz EM. The AP2/EREBP family of plant transcription
	+	factors. Biol Chem. 1998 Jun;379(6):633-46. Review. PubMed PMID: 9687012.
	+	</ref>
	+	</references>

← Older revision		Revision as of 05:54, 30 December 2016
Line 1:		Line 1:
−	~~Please input one-sentence summary here.~~

−	~~==Annotated Information==~~
−	~~===Function===~~
−	~~GPA3 encodes a plant-specific kelch-repeat protein that is localized to~~
−	the trans-Golgi networks, DVs, and PSVs in the developing endosperm. In vitro and in vivo experiments verified that GPA3 directly interacts with the rice Rab5a-guanine exchange factor VPS9a and forms a regulatory complex with Rab5a via VPS9a.GPA3 acts synergistically with Rab5a and VPS9a to regulate DV-mediated post-Golgi traffic in rice<ref name="ref1" />.
−
−	~~===Mutations===~~
−	*Phenotypic Characterization of the gpa3 Mutant
−	~~The gpa3 plants exhibited no visible abnormalities before the grainfilling~~
−	stage, such as plant height, tiller number, and heading date.After fertilization, the gpa3 mutant exhibited a markedly slower grain-filling rate (Figure 1A) and eventually produced a shrunken and floury endosperm (Figure 1B),Scanning electron microscopy analysis revealed that the wild-type endosperm was filled with densely packed, polyhedral starch granules, but endosperm of the gpa3 mutant was packed with round, irregularly arranged compound starch granules (Figure 1C)<ref name="ref1" />.SDS-PAGE and immunoblot analyses revealed that the accumulation of prolamins was comparable in the dry seeds of the wild type and the gpa3 mutant. However, the gpa3 mutant seeds exhibited increased accumulation of 57-kD proglutelins, accompanied by reduced accumulation of the mature acidic and basic subunits as well as a-globulins, compared with wild-type seeds
−	(Figures 1D and 1E),In addition, immunoblot analysis using isoform specific antibodies revealed increased accumulation of proglutelins for all glutelin subfamilies(GluA, GluB, and GluC; <ref name="ref2" />), accompanied by decreased accumulation of their respective acidic subunits in the gpa3 mutant (Figure 1F), suggesting that a defect in a regulatory
−	~~factor rather than glutelin structural genes may be responsible for the gpa3 mutant phenotypes(Figure 1)<ref name="ref1" />.~~
−	~~[[File:Figure 1.png\|right\|thumb\|320px\|'''Figure 1.''' ''Phenotypic Analyses of the gpa3 Mutant.<ref name="ref1" />'']]~~
−	*Abnormal Deposition of Glutelins and a-Globulins in the gpa3 Mutant
−	As shown in Figures 2A and 2B, Coomassie blue staining showed that the storage proteins were most abundant in the subaleurone layer of endosperm in both the wild type and the gpa3 mutant.numerous glutelin- and a-globulin–containing protein granules distributed near the cell periphery in the gpa3 mutant endosperm but not in wild-type endosperm (Figures 2C to 2F)(Figure 2)<ref name="ref1" />.
−	[[File:the Wild Type and the gpa3 Mutant.png\|right\|thumb\|320px\|'''Figure2.''' ''Light and Immunofluorescence Microscopy Images of Protein Bodies in the Subaleurone Cells of the Wild Type and the gpa3 Mutant.<ref name="ref1" />'']]
−
−	~~===Expression===~~
−	~~the phenotypes of the gpa3 mutant were restricted to endosperm, GPA3 expression was detected in all tissues examined, including root, stem,~~
−	~~leaf, leaf sheath, panicle, and endosperm, with highest accumulation~~
−	in the leaf(Figure 3G).During endosperm development,the expression of GPA3 was low at an early stage, then peaked at;18 DAF, and slowly decreased after 21 DAF (Figure 3H).Thus,GPA3 encodes a plant-specific kelch-repeat
−	~~protein and that it is broadly expressed inmultiple organs and tissues.~~
−	~~[[File:the expression of GPA3.png\|right\|thumb\|320px\|'''Figure3.''' ''Expression Analysis of GPA3.<ref name="ref1" />'']]~~
−
−	~~===Evolution===~~
−	~~Please input evolution information here~~
−
−
−
−
−
−	~~===Localization===~~
−	To determine the subcellular localization of the GPA3 protein,P35S:GPA3-GFP was transiently expressedin Arabidopsis protoplasts.As expected, GFP itself was distributed evenly in the cytoplasm and the nucleus, whereas the GPA3-GFP fusion protein was mainly localized to the cytoplasm and to punctate compartments in the cytosol. Moreover,we observed colocalization of various combinations of GPA3 fused with either fluorescent protein (GFP or mCherry) or a Flag tag at the N terminus or C terminus in Arabidopsis protoplasts.To determine the nature of these punctate compartments, we coexpressed GPA3-GFP and fluorescent marker proteins characteristic for the Golgi apparatus<ref name="ref3" /> , the TGN<ref name="ref4" /> and the PVC<ref name="ref5" /> . As shown in Figures 4A to 4C, the punctate compartments of GPA3-GFP were obviously distinct from the Golgi but partially overlapped with the TGN and PVC. Furthermore, correlation analysis using the Pearson-Spearman correlation (PSC) plugin for ImageJ revealed strong correlation between GPA3-GFP and the PVC marker , but the correlation between GPA3-GFP and the TGN marker appeared to be weaker.Furthermore, immunoelectron microscopy analysis with anti-GFP antibodies revealed that GPA3-GFP was targeted to the TGN, DVs, and PBIIs (Figure 4D). Together, these data indicated that GPA3 is localized to various post-Golgi compartments irrespective of the cell types(Figure 4).
−	[[File:Subcellular Localization of GPA3 in Arabidopsis Protoplasts and Developing Subaleurone Cells.png\|right\|thumb\|320px\|'''Figure 4.''' ''Figure 4. Subcellular Localization of GPA3 in Arabidopsis Protoplasts and Developing Subaleurone Cells.<ref name="ref1" />'']]
−
−	~~==Labs working on this gene==~~
−	*State Key Laboratory for Crop Genetics and Germplasm Enhancement, Jiangsu Plant Gene Engineering Research Center, Nanjing Agricultural University, Nanjing 210095, China
−	*National Key Facility for Crop Gene Resources and Genetic Improvement, Institute of Crop Science, Chinese Academy of Agricultural Sciences, Beijing 100081, China
−	*School of Life Sciences, Centre for Cell and Developmental Biology, Chinese University of Hong Kong, New Territories, Hong Kong 999077, China
−	*College of Life Sciences, Nanjing Agricultural University, Nanjing 210095, China
−
−	~~==References==~~
−	~~<references>~~
−	* <ref name="ref1">
−	~~Yulong Ren,Yihua Wang,Feng Liu,et al.GLUTELIN PRECURSOR ACCUMULATION3 Encodes a Regulator of Post-Golgi Vesicular Traffic Essential for~~
−	~~Vacuolar Protein Sorting in Rice Endosperm[J].Plant cell,2014,26: 410–425.~~
−	~~</ref>~~
−	* <ref name="ref2">
−	~~Takemoto, Y., Coughlan, S.J., Okita,et al.The rice mutant esp2 greatly~~
−	~~accumulates the glutelin precursor and deletes the protein disulfide~~
−	~~isomerase[J]. Plant Physiol,2002, 128: 1212–1222.~~
−	~~</ref>~~
−	* <ref name="ref3">
−	~~Tse, Y.C., Mo, B., Hillmer,et al.Identification of multivesicular bodies as~~
−	~~prevacuolar compartments in Nicotiana tabacum BY-2 cells[J]. Plant Cell,2004, 16: 672–693.~~
−	~~</ref>~~
−	* <ref name="ref4">
−	~~Lam, S.K., Siu, C.L., Hillmer,et al.Rice SCAMP1 defines clathrin-coated, trans-Golgi-located tubular-vesicular structures as an early endosome in~~
−	~~tobacco BY-2 cells[J]. Plant Cell ,2007b,19: 296–319.~~
−	~~</ref>~~
−	* <ref name="ref5">
−	Miao, Y., Yan, P.K., Kim, H.,et al.Localization of green fluorescent protein fusions with the seven Arabidopsis vacuolar sorting receptors to prevacuolar compartments in tobacco BY-2 cells[J].Plant Physiol,2006,142: 945–962.
−
−	~~==Structured Information==~~
−
−	~~[[Category:Genes]]~~
−	~~[[Category:Japonica mRNA]]~~
−	~~[[Category:Oryza Sativa Japonica Group]]~~
−	~~[[Category:Japonica Genes]]~~
−	~~[[Category:Japonica Chromosome 2]]~~
−	~~[[Category:Chromosome 2]]~~

@@ Line 64: / Line 64: @@
 ==Structured Information==
 [[Category:Genes]]
 [[Category:Japonica mRNA]]

@@ Line 42: / Line 42: @@
 ==References==
-Please input cited references here.
+<references>
 ==Structured Information==

@@ Line 10: / Line 10: @@
 The gpa3 plants exhibited no visible abnormalities before the grainfilling
 stage, such as plant height, tiller number, and heading date.After fertilization, the gpa3 mutant exhibited a markedly slower grain-filling rate (Figure 1A) and eventually produced a shrunken and floury endosperm (Figure 1B),Scanning electron microscopy analysis revealed that the wild-type endosperm was filled with densely packed, polyhedral starch granules, but endosperm of the gpa3 mutant was packed with round, irregularly arranged compound starch granules (Figure 1C)<ref name="ref1" />.SDS-PAGE and immunoblot analyses revealed that the accumulation of prolamins was comparable in the dry seeds of the wild type and the gpa3 mutant. However, the gpa3 mutant seeds exhibited increased accumulation of 57-kD proglutelins, accompanied by reduced accumulation of the mature acidic and basic subunits as well as a-globulins, compared with wild-type seeds
-(Figures 1D and 1E),In addition, immunoblot analysis using isoform specific antibodies revealed increased accumulation of proglutelins for all glutelin subfamilies(GluA, GluB, and GluC; <ref name="ref1" />), accompanied by decreased accumulation of their respective acidic subunits in the gpa3 mutant (Figure 1F), suggesting that a defect in a regulatory
+(Figures 1D and 1E),In addition, immunoblot analysis using isoform specific antibodies revealed increased accumulation of proglutelins for all glutelin subfamilies(GluA, GluB, and GluC; <ref name="ref2" />), accompanied by decreased accumulation of their respective acidic subunits in the gpa3 mutant (Figure 1F), suggesting that a defect in a regulatory
 factor rather than glutelin structural genes may be responsible for the gpa3 mutant phenotypes(Figure 1)<ref name="ref1" />.
 [[File:Figure 1.png|right|thumb|320px|'''Figure 1.''' ''Phenotypic Analyses of the gpa3 Mutant.<ref name="ref1" />'']]

@@ Line 32: / Line 32: @@
 ===Localization===
-To determine the subcellular localization of the GPA3 protein,P35S:GPA3-GFP was transiently expressedin Arabidopsis protoplasts.As expected, GFP itself was distributed evenly in the cytoplasm and the nucleus, whereas the GPA3-GFP fusion protein was mainly localized to the cytoplasm and to punctate compartments in the cytosol. Moreover,we observed colocalization of various combinations of GPA3 fused with either fluorescent protein (GFP or mCherry) or a Flag tag at the N terminus or C terminus in Arabidopsis protoplasts.To determine the nature of these punctate compartments, we coexpressed GPA3-GFP and fluorescent marker proteins characteristic for the Golgi apparatus , the TGN and the PVC . As shown in Figures 4A to 4C, the punctate compartments of GPA3-GFP were obviously distinct from the Golgi but partially overlapped with the TGN and PVC. Furthermore, correlation analysis using the Pearson-Spearman correlation (PSC) plugin for ImageJ revealed strong correlation between GPA3-GFP and the PVC marker , but the correlation between GPA3-GFP and the TGN marker appeared to be weaker.Furthermore, immunoelectron microscopy analysis with anti-GFP antibodies revealed that GPA3-GFP was targeted to the TGN, DVs, and PBIIs (Figure 4D). Together, these data indicated that GPA3 is localized to various post-Golgi compartments irrespective of the cell types(Figure 4).
+To determine the subcellular localization of the GPA3 protein,P35S:GPA3-GFP was transiently expressedin Arabidopsis protoplasts.As expected, GFP itself was distributed evenly in the cytoplasm and the nucleus, whereas the GPA3-GFP fusion protein was mainly localized to the cytoplasm and to punctate compartments in the cytosol. Moreover,we observed colocalization of various combinations of GPA3 fused with either fluorescent protein (GFP or mCherry) or a Flag tag at the N terminus or C terminus in Arabidopsis protoplasts.To determine the nature of these punctate compartments, we coexpressed GPA3-GFP and fluorescent marker proteins characteristic for the Golgi apparatus<ref name="ref3" /> , the TGN<ref name="ref4" /> and the PVC<ref name="ref5" /> . As shown in Figures 4A to 4C, the punctate compartments of GPA3-GFP were obviously distinct from the Golgi but partially overlapped with the TGN and PVC. Furthermore, correlation analysis using the Pearson-Spearman correlation (PSC) plugin for ImageJ revealed strong correlation between GPA3-GFP and the PVC marker , but the correlation between GPA3-GFP and the TGN marker appeared to be weaker.Furthermore, immunoelectron microscopy analysis with anti-GFP antibodies revealed that GPA3-GFP was targeted to the TGN, DVs, and PBIIs (Figure 4D). Together, these data indicated that GPA3 is localized to various post-Golgi compartments irrespective of the cell types(Figure 4).
 [[File:Subcellular Localization of GPA3 in Arabidopsis Protoplasts and Developing Subaleurone Cells.png|right|thumb|320px|'''Figure 4.''' ''Figure 4. Subcellular Localization of GPA3 in Arabidopsis Protoplasts and Developing Subaleurone Cells.<ref name="ref1" />'']]

@@ Line 9: / Line 9: @@
 *Phenotypic Characterization of the gpa3 Mutant
 The gpa3 plants exhibited no visible abnormalities before the grainfilling
-stage, such as plant height, tiller number, and heading date.After fertilization, the gpa3 mutant exhibited a markedly slower grain-filling rate (Figure 1A) and eventually produced a shrunken and floury endosperm (Figure 1B),Scanning electron microscopy analysis revealed that the wild-type endosperm was filled with densely packed, polyhedral starch granules, but endosperm of the gpa3 mutant was packed with round, irregularly arranged compound starch granules (Figure 1C).SDS-PAGE and immunoblot analyses revealed that the accumulation of prolamins was comparable in the dry seeds of the wild type and the gpa3 mutant. However, the gpa3 mutant seeds exhibited increased accumulation of 57-kD proglutelins, accompanied by reduced accumulation of the mature acidic and basic subunits as well as a-globulins, compared with wild-type seeds
+stage, such as plant height, tiller number, and heading date.After fertilization, the gpa3 mutant exhibited a markedly slower grain-filling rate (Figure 1A) and eventually produced a shrunken and floury endosperm (Figure 1B),Scanning electron microscopy analysis revealed that the wild-type endosperm was filled with densely packed, polyhedral starch granules, but endosperm of the gpa3 mutant was packed with round, irregularly arranged compound starch granules (Figure 1C)<ref name="ref1" />.SDS-PAGE and immunoblot analyses revealed that the accumulation of prolamins was comparable in the dry seeds of the wild type and the gpa3 mutant. However, the gpa3 mutant seeds exhibited increased accumulation of 57-kD proglutelins, accompanied by reduced accumulation of the mature acidic and basic subunits as well as a-globulins, compared with wild-type seeds
 (Figures 1D and 1E),In addition, immunoblot analysis using isoform specific antibodies revealed increased accumulation of proglutelins for all glutelin subfamilies(GluA, GluB, and GluC; Takemoto et al., 2002), accompanied by decreased accumulation of their respective acidic subunits in the gpa3 mutant (Figure 1F), suggesting that a defect in a regulatory
-factor rather than glutelin structural genes may be responsible for the gpa3 mutant phenotypes(Figure 1).
+factor rather than glutelin structural genes may be responsible for the gpa3 mutant phenotypes(Figure 1)<ref name="ref1" />.
 [[File:Figure 1.png|right|thumb|320px|'''Figure 1.''' ''Phenotypic Analyses of the gpa3 Mutant.<ref name="ref1" />'']]
 *Abnormal Deposition of Glutelins and a-Globulins in the gpa3 Mutant
-As shown in Figures 2A and 2B, Coomassie blue staining showed that the storage proteins were most abundant in the subaleurone layer of endosperm in both the wild type and the gpa3 mutant.numerous glutelin- and a-globulin–containing protein granules distributed near the cell periphery in the gpa3 mutant endosperm but not in wild-type endosperm (Figures 2C to 2F)(Figure 2).
+As shown in Figures 2A and 2B, Coomassie blue staining showed that the storage proteins were most abundant in the subaleurone layer of endosperm in both the wild type and the gpa3 mutant.numerous glutelin- and a-globulin–containing protein granules distributed near the cell periphery in the gpa3 mutant endosperm but not in wild-type endosperm (Figures 2C to 2F)(Figure 2)<ref name="ref1" />.
 [[File:the Wild Type and the gpa3 Mutant.png|right|thumb|320px|'''Figure2.''' ''Light and Immunofluorescence Microscopy Images of Protein Bodies in the Subaleurone Cells of the Wild Type and the gpa3 Mutant.<ref name="ref1" />'']]

@@ Line 4: / Line 4: @@
 ===Function===
 GPA3 encodes a plant-specific kelch-repeat protein that is localized to
-the trans-Golgi networks, DVs, and PSVs in the developing endosperm. In vitro and in vivo experiments verified that GPA3 directly interacts with the rice Rab5a-guanine exchange factor VPS9a and forms a regulatory complex with Rab5a via VPS9a.GPA3 acts synergistically with Rab5a and VPS9a to regulate DV-mediated post-Golgi traffic in rice.
+the trans-Golgi networks, DVs, and PSVs in the developing endosperm. In vitro and in vivo experiments verified that GPA3 directly interacts with the rice Rab5a-guanine exchange factor VPS9a and forms a regulatory complex with Rab5a via VPS9a.GPA3 acts synergistically with Rab5a and VPS9a to regulate DV-mediated post-Golgi traffic in rice<ref name="ref1" />.
 ===Mutations===
 *Phenotypic Characterization of the gpa3 Mutant