Os03g0262900 - Revision history

Rice2012: /* Structured Information */

2015-06-12T05:38:39Z

‎Structured Information

Gretaleigh: /* Knowledge Extension */

2014-05-15T11:21:23Z

‎Knowledge Extension

Gretaleigh: /* Knowledge Extension */

2014-05-15T11:19:32Z

‎Knowledge Extension

Gretaleigh: /* Wild Type VS. Mutant */

2014-05-15T11:13:59Z

‎Wild Type VS. Mutant

Gretaleigh: /* Evolution */

2014-05-15T11:08:01Z

‎Evolution

Gretaleigh: /* Expression */

2014-05-15T11:05:17Z

‎Expression

Gretaleigh: /* Wild Type VS. Mutant */

2014-05-15T11:01:32Z

‎Wild Type VS. Mutant

Gretaleigh: /* Wild Type VS. Mutant */

2014-05-15T11:00:16Z

‎Wild Type VS. Mutant

Gretaleigh: /* Expression */

2014-05-15T10:37:29Z

‎Expression

Gretaleigh: /* Expression */

2014-05-15T10:36:13Z

‎Expression

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

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 ===Knowledge Extension===
-In the rice endosperm cells, glutelins are synthesized on rough endoplasmic reticulum as proglutelins and are sorted to the protein storage vacuoles (PSVs) called protein body IIs (PBIIs), where they are converted to the mature forms.Dense vesicle (DV)-mediated trafficking of proglutelins in rice seeds has been proposed, but the post-Golgi control of this process is largely unknown. OsVPS9A and OsRAB5A may work together and play a regulatory role in DV-mediated post-Golgi proglutelin trafficking to PBII (PSV).
+In the rice endosperm cells, glutelins are synthesized on rough endoplasmic reticulum as proglutelins and are sorted to the protein storage vacuoles (PSVs) called protein body IIs (PBIIs), where they are converted to the mature forms.Dense vesicle (DV)-mediated trafficking of proglutelins in rice seeds has been proposed, but the post-Golgi control of this process is largely unknown. OsVPS9A and OsRAB5A may work together and play a regulatory role in DV-mediated post-Golgi proglutelin trafficking to PBII (PSV)<ref name="ref3" />.
 ==Labs working on this gene==

← Older revision		Revision as of 11:19, 15 May 2014
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	===Knowledge Extension===		===Knowledge Extension===
		+	In the rice endosperm cells, glutelins are synthesized on rough endoplasmic reticulum as proglutelins and are sorted to the protein storage vacuoles (PSVs) called protein body IIs (PBIIs), where they are converted to the mature forms.Dense vesicle (DV)-mediated trafficking of proglutelins in rice seeds has been proposed, but the post-Golgi control of this process is largely unknown. OsVPS9A and OsRAB5A may work together and play a regulatory role in DV-mediated post-Golgi proglutelin trafficking to PBII (PSV).

	==Labs working on this gene==		==Labs working on this gene==

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 [[File:Pair3_图片3.jpg|right|thumb|275px|'''Figure 2.''' ' Immunoblot analysis of the seed protein from glup6 lines using anti-GLUP6/GEF antibody.(from reference) <ref name="ref2" />.'']]
 [[File:Pair3_图片.jpg|right|thumb|275px|'''Figure 3.''' '  Characterization of the gpa2 Mutant..(from reference) <ref name="ref3" />.'']]
+*''GLUP6 / GEF'' in Fukuda's research<ref name="ref2" /> and ''OsVPS9A/GPA2'' in Liu's research<ref name="ref3" /> locate in the same gene locus.
 *The ''glup6'' mutant accumulates large amounts of proglutelin<ref name="ref2" />. Figure 1A shows the profiles of total seed protein samples from three independent ''glup6'' mutant lines, EM939, EM1327, and EM1484, as well as from the wildtype. All three ''glup6'' lines contained elevated amounts of the 57-kD proglutelin polypeptide compared with the wild type. The change in the proglutelin levels between the wild type and the ''glup6'' mutants was readily discernible by immunoblot analysis (Fig. 1B). Figure 1C shows that the grain morphology is also significantly altered in the ''glup6'' mutants. All three mutant lines exhibited a floury endosperm.
 *Immunoblot analysis using an antibody raised against GLUP6/GEF revealed two reacting polypeptide bands in developing wild-type seeds with the bottom band missing in all ''glup6'' lines (Fig. 2)<ref name="ref2" />. The theoretical molecular mass of GLUP6/GEF is 53.8 kD, a value in close agreement with the measured molecular size of the bottom polypeptide band. The ubiquitous presence of the top polypeptide band in Figure 2 may be due to another GEF-related protein. As all ''glup6'' lines contain nonsense mutations, even one close to the C terminus(EM1327), the lack of accumulated truncated polypeptides indicates that the polypeptide and the mRNA are unstable, the latter macromolecule likely degraded by nonsense-mediated mRNA decay.

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 *In order to elucidate the function of GLUP6/GEF in the intracellular transport of proglutelins, the endosperm of ''glup6'' lines was analyzed by immunofluorescence microscopy (Fig.4).In wild-type endosperm, protein bodies containing prolamines (protein body type I [PB-I]) and glutelins and a-globulins (PB-II) increased in size and number as the seeds developed (Fig. 4,Aand B). In ''glup6'' lines EM939 and EM1327, one or more large distended structures reactive to glutelin antibodies were conspicuously observed close to the cell wall (Fig. 4, B and C)<ref name="ref2" />.
-===Evolution===
+===Knowledge Extension===
 ==Labs working on this gene==

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 ===Expression===
-[[File:Pair3_图片4.jpg|right|thumb|275px|'''Figure 3.''' ' The distribution of storage proteins in the wild type (A and D) and glup6 mutant lines EM939 (Gln-140 stop; B and E) and EM1327 (Gln-262 stop; C and F) as viewed by immunofluorescence microscopy.(from reference) <ref name="ref2" />.'']]
+[[File:Pair3_图片4.jpg|right|thumb|275px|'''Figure 4.''' ' The distribution of storage proteins in the wild type (A and D) and glup6 mutant lines EM939 (Gln-140 stop; B and E) and EM1327 (Gln-262 stop; C and F) as viewed by immunofluorescence microscopy.(from reference) <ref name="ref2" />.'']]
 *The full-length open reading frame of Os03g0262900 was amplified with gene-specificprimers usingcomplementary DNA (cDNA) reverse transcribed from mRNA extracted from the immature seeds of the wild-type Taichung65 as a template. Sequencing analysis of the amplified single band demonstrated that the ''GLUP6'' candidate gene possessed a coding sequence of 1,443 bp coding for 480 deduced amino acids spanning over five exons<ref name="ref1" />.
-*In order to elucidate the function of GLUP6/GEF in the intracellular transport of proglutelins, the endosperm of ''glup6'' lines was analyzed by immunofluorescence microscopy (Fig.3).In wild-type endosperm, protein bodies containing prolamines (protein body type I [PB-I]) and glutelins and a-globulins (PB-II) increased in size and number as the seeds developed (Fig. 3,Aand B). In ''glup6'' lines EM939 and EM1327, one or more large distended structures reactive to glutelin antibodies were conspicuously observed close to the cell wall (Fig. 3, B and C)<ref name="ref2" />.
+*In order to elucidate the function of GLUP6/GEF in the intracellular transport of proglutelins, the endosperm of ''glup6'' lines was analyzed by immunofluorescence microscopy (Fig.4).In wild-type endosperm, protein bodies containing prolamines (protein body type I [PB-I]) and glutelins and a-globulins (PB-II) increased in size and number as the seeds developed (Fig. 4,Aand B). In ''glup6'' lines EM939 and EM1327, one or more large distended structures reactive to glutelin antibodies were conspicuously observed close to the cell wall (Fig. 4, B and C)<ref name="ref2" />.
 ===Evolution===