Difference between revisions of "Os02g0656600"
(→Function) |
(→Mutations) |
||
| Line 10: | Line 10: | ||
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).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 | (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. | + | factor rather than glutelin structural genes may be responsible for the gpa3 mutant phenotypes(Figure 1). |
| + | [[File:Figure 1.png|right|thumb|320px|'''Figure 2.''' ''Figure 1. Phenotypic Analyses of the gpa3 Mutant.<ref name="ref1" />'']] | ||
*Abnormal Deposition of Glutelins and a-Globulins in the gpa3 Mutant | *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). | + | 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). |
| + | [[File:Figure 2.png|right|thumb|320px|'''Figure 2.''' ''Figure 2. Light and Immunofluorescence Microscopy Images of Protein Bodies in the Subaleurone Cells of the Wild Type and the gpa3 Mutant.<ref name="ref2" />'']] | ||
===Expression=== | ===Expression=== | ||
Revision as of 08:06, 27 May 2014
Please input one-sentence summary here.
Contents
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.
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).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).
- 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).
Expression
Please input expression information here.
Evolution
Please input evolution information here.
You can also add sub-section(s) at will.
Labs working on this gene
Please input related labs here.
References
Please input cited references here.
Structured Information
| Gene Name |
Os02g0656600 |
|---|---|
| Description |
Similar to Dehydration responsive element binding protein 2B (DREB2B protein) |
| Version |
NM_001054162.1 GI:115447694 GeneID:4330202 |
| Length |
1080 bp |
| Definition |
Oryza sativa Japonica Group Os02g0656600, complete gene. |
| Source |
Oryza sativa Japonica Group ORGANISM Oryza sativa Japonica Group
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP
clade; Ehrhartoideae; Oryzeae; Oryza.
|
| Chromosome | |
| Location |
Chromosome 2:27411434..27412513 |
| Sequence Coding Region |
27411524..27412387 |
| Expression | |
| Genome Context |
<gbrowseImage1> name=NC_008395:27411434..27412513 source=RiceChromosome02 preset=GeneLocation </gbrowseImage1> |
| Gene Structure |
<gbrowseImage2> name=NC_008395:27411434..27412513 source=RiceChromosome02 preset=GeneLocation </gbrowseImage2> |
| Coding Sequence |
<cdnaseq>atggaagctgccgcgatccatgcgcccaccaccaccacctcctccgactccggctcgtgcgtcaccaatggcacgcgagagaagcgcgagatctctaagcacaagcagctcaagcggaagaggagcacctctcctgctcctcctcccggctgcggcggcggccaaggacaggaagcggcggtggagactgacgctgacgctggcgccgccggcgaggaggagagcagcagctgcggtggcgctggcgccggcgagggcgagcgcaagaggggtgacgccggcaggcacccgtcgtaccgcggcgtgaggcggcggagctggggcaagtgggtgtcggagatccgcgagccgcgcaagaagtcgcgcatctggctcggcaccttcccgacggcggagatggccgcgcgcgcgcacgacgtggccgcgctcgccatcaagggccgcgccgcgcacctcaacttcccgagcctcgcccacacgctcccgcgcccggcctccacctcaccctccgacatccaggccgccgccgccctcgccgcagctgcagccgccaccgaccaatgcgagtcctcctcctctgccgtcgccgccgccaccgccaccgacgccgaggcggcggagtccacctcgtcggccgcggccagcccgtgcgccgccaccagcagcgtcgaggagaacgcgctgttcgacctgcccgaccttctcctcgacctgagcgacgggctctggtgctcacccgtctggacgacagcgccggccgatcagtacgacgccggcgacgacggcgacgacgccgcggcgccgctcctgtgggccgagcagtgctggatggacgccccagcggcgcccgtgcagcctgactaa</cdnaseq> |
| Protein Sequence |
<aaseq>MEAAAIHAPTTTTSSDSGSCVTNGTREKREISKHKQLKRKRSTS PAPPPGCGGGQGQEAAVETDADAGAAGEEESSSCGGAGAGEGERKRGDAGRHPSYRGV RRRSWGKWVSEIREPRKKSRIWLGTFPTAEMAARAHDVAALAIKGRAAHLNFPSLAHT LPRPASTSPSDIQAAAALAAAAAATDQCESSSSAVAAATATDAEAAESTSSAAASPCA ATSSVEENALFDLPDLLLDLSDGLWCSPVWTTAPADQYDAGDDGDDAAAPLLWAEQCW MDAPAAPVQPD</aaseq> |
| Gene Sequence |
<dnaseqindica>91..954#cctggaaggaagcgcatctccttcctgcggtattctgtgtgcctctctctctctctctctcctccaccttgtcgtagagaggaggcggccatggaagctgccgcgatccatgcgcccaccaccaccacctcctccgactccggctcgtgcgtcaccaatggcacgcgagagaagcgcgagatctctaagcacaagcagctcaagcggaagaggagcacctctcctgctcctcctcccggctgcggcggcggccaaggacaggaagcggcggtggagactgacgctgacgctggcgccgccggcgaggaggagagcagcagctgcggtggcgctggcgccggcgagggcgagcgcaagaggggtgacgccggcaggcacccgtcgtaccgcggcgtgaggcggcggagctggggcaagtgggtgtcggagatccgcgagccgcgcaagaagtcgcgcatctggctcggcaccttcccgacggcggagatggccgcgcgcgcgcacgacgtggccgcgctcgccatcaagggccgcgccgcgcacctcaacttcccgagcctcgcccacacgctcccgcgcccggcctccacctcaccctccgacatccaggccgccgccgccctcgccgcagctgcagccgccaccgaccaatgcgagtcctcctcctctgccgtcgccgccgccaccgccaccgacgccgaggcggcggagtccacctcgtcggccgcggccagcccgtgcgccgccaccagcagcgtcgaggagaacgcgctgttcgacctgcccgaccttctcctcgacctgagcgacgggctctggtgctcacccgtctggacgacagcgccggccgatcagtacgacgccggcgacgacggcgacgacgccgcggcgccgctcctgtgggccgagcagtgctggatggacgccccagcggcgcccgtgcagcctgactaattaagccaatccacctgctccgactcgccggccggccattgcaccggttgggttggtcgcagcagtcaacctatcgacaccatgggcgtctttttcttttctctctgtttttttttcttttttgga</dnaseqindica> |
| External Link(s) |