Os03g0766100 - Revision history

192.168.72.52: /* Structured Information */

2015-06-12T06:03:13Z

‎Structured Information

Littlescrew: /* Expression */

2014-06-04T14:33:08Z

‎Expression

Littlescrew: /* Expression */

2014-06-04T14:32:11Z

‎Expression

Littlescrew: /* Expression */

2014-06-04T08:29:10Z

‎Expression

Littlescrew at 08:26, 4 June 2014

2014-06-04T08:26:31Z

Littlescrew: /* Expression */

2014-06-04T08:23:39Z

‎Expression

Littlescrew: /* Expression */

2014-06-04T08:08:52Z

‎Expression

Littlescrew: /* Expression */

2014-06-04T07:22:56Z

‎Expression

Littlescrew: /* Expression */

2014-06-04T07:21:57Z

‎Expression

Littlescrew: /* Labs working on this gene */

2014-06-04T05:53:17Z

‎Labs working on this gene

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

@@ Line 11: / Line 11: @@
 Immunofluorescence light microscopy confirmed the spatial distribution of these prolamins within the PBs. CysR10 was visualized as small particles when labeled by anti-CysR10 followed by rhodamine-conjugated secondary antibodies (Fig. 1D). The distribution of CysR10 co-localized with CysP13, which was visualized with fluorescein isothiocyanate (FITC)-conjugated secondary antibodies (Fig. 1 E, F arrows). CysR10 was observed at the center of the PBs, whereas the distribution of CysP13 was more varied. Details about the spatial relationship between the prolamins were confirmed by immunofluorescence microscopy images from developing endosperm at 3 WAF (Fig. 2). They show that PB-I is composed of a center core of CysR10, surrounded by a middle layer of a mixture of CysR10 and CysP13, and then followed by a peripheral layer containing CysP13 devoid of CysR10. By immunoelectron microscopy, a more detailed structure of PB-I can be analyzed through its ultrastructure during different stages of seed development (at 5 DAF, 1 WAF, 2 WAF, and 3 WAF), then the Schematic images of PB-I structure during rice endosperm development can be obtained (Fig. 5).
 [[File:Fig. 2.jpg|right|thumb|430px|'''Fig 2.''' ''Fig. 2 Immunofluorescence microscopy of serial sections of PB-Is obtained from developing rice endosperm at 3 WAF (from reference) <ref name="ref2" />.. The numbers at the left of the image denote the order of the sections. The PBs in each section were labeled with antibodies against CysR10 and CysP13. The CysR10–antibody interactions were visualized with rhodamine-conjugated secondary antibodies (A–D), while those for CysP13s were visualized with FITC-conjugated secondary antibodies (E–H). (I–L) Merged images. The arrow indicates the location of the same PB in the serial sections. Bars: 4mm.'']]
-[[File:Crp10.jpg|right|thumb|430px|'''Fig 5.'''''Fig. 5 (I) Schematic images of PB-I structure during rice endosperm development(from reference) <ref name="ref2" />.'']]
+[[File:Crp10.jpg|right|thumb|430px|'''Fig 5.'''''(I) Schematic images of PB-I structure during rice endosperm development(from reference) <ref name="ref2" />.'']]
 The prolamin-containing PB-Is were non-spherical in the CysR10-repressed endosperm, because CysR10 is required for forming PB-Is into the spherical shape and for the compact size, and that it not only forms the central core but also interacts with other Cys-rich prolamins to assemble the concentric ring structure within the PB-I. In addition, RNAi suppression of CysR10 slightly reduced the expression level of CysP13, but CysR16 and CysR14 were normal or slightly higher amounts. However, Kawakatsu ''et al.''<ref name="ref6" /> reported that their 10 kDa prolamin-suppressed plant accumulated substantially higher levels (about three times compared with the wild type) of CysR14 (RM1 and RM9) and CysR16 (RP16) prolamins than normal, although CysP13 (RM2 and RM4) prolamins were lower amounts. This different result may due to the differences of the methods used to regulate down the CysR10 expression level <ref name="ref7" />. One is the conventional RNAi method with the inverted CysR10 open reading frame, and the other one is the expression of a modified human Glucagon-like peptide-1 (GLP-1) to regulate down the target proteins. This elevated levels of CysR14 and CysR16 may compensate for the loss of CysR10 and contribute to form a rigid normal sized PB-I. Another consist result came from an endosperm storage protein mutant that contains reduced levels of CysR16, CysR14 and CysR10 and displays abnormal large PBIs.

@@ Line 11: / Line 11: @@
 Immunofluorescence light microscopy confirmed the spatial distribution of these prolamins within the PBs. CysR10 was visualized as small particles when labeled by anti-CysR10 followed by rhodamine-conjugated secondary antibodies (Fig. 1D). The distribution of CysR10 co-localized with CysP13, which was visualized with fluorescein isothiocyanate (FITC)-conjugated secondary antibodies (Fig. 1 E, F arrows). CysR10 was observed at the center of the PBs, whereas the distribution of CysP13 was more varied. Details about the spatial relationship between the prolamins were confirmed by immunofluorescence microscopy images from developing endosperm at 3 WAF (Fig. 2). They show that PB-I is composed of a center core of CysR10, surrounded by a middle layer of a mixture of CysR10 and CysP13, and then followed by a peripheral layer containing CysP13 devoid of CysR10. By immunoelectron microscopy, a more detailed structure of PB-I can be analyzed through its ultrastructure during different stages of seed development (at 5 DAF, 1 WAF, 2 WAF, and 3 WAF), then the Schematic images of PB-I structure during rice endosperm development can be obtained (Fig. 5).
 [[File:Fig. 2.jpg|right|thumb|430px|'''Fig 2.''' ''Fig. 2 Immunofluorescence microscopy of serial sections of PB-Is obtained from developing rice endosperm at 3 WAF (from reference) <ref name="ref2" />.. The numbers at the left of the image denote the order of the sections. The PBs in each section were labeled with antibodies against CysR10 and CysP13. The CysR10–antibody interactions were visualized with rhodamine-conjugated secondary antibodies (A–D), while those for CysP13s were visualized with FITC-conjugated secondary antibodies (E–H). (I–L) Merged images. The arrow indicates the location of the same PB in the serial sections. Bars: 4mm.'']]
 The prolamin-containing PB-Is were non-spherical in the CysR10-repressed endosperm, because CysR10 is required for forming PB-Is into the spherical shape and for the compact size, and that it not only forms the central core but also interacts with other Cys-rich prolamins to assemble the concentric ring structure within the PB-I. In addition, RNAi suppression of CysR10 slightly reduced the expression level of CysP13, but CysR16 and CysR14 were normal or slightly higher amounts. However, Kawakatsu ''et al.''<ref name="ref6" /> reported that their 10 kDa prolamin-suppressed plant accumulated substantially higher levels (about three times compared with the wild type) of CysR14 (RM1 and RM9) and CysR16 (RP16) prolamins than normal, although CysP13 (RM2 and RM4) prolamins were lower amounts. This different result may due to the differences of the methods used to regulate down the CysR10 expression level <ref name="ref7" />. One is the conventional RNAi method with the inverted CysR10 open reading frame, and the other one is the expression of a modified human Glucagon-like peptide-1 (GLP-1) to regulate down the target proteins. This elevated levels of CysR14 and CysR16 may compensate for the loss of CysR10 and contribute to form a rigid normal sized PB-I. Another consist result came from an endosperm storage protein mutant that contains reduced levels of CysR16, CysR14 and CysR10 and displays abnormal large PBIs.

@@ Line 10: / Line 10: @@
 [[File:Fig. 1.jpg|right|thumb|430px|'''Fig 1.''' ''Distribution of CysR10 and CysP13 in PB-Is of developing rice endosperm at 3 WAF (from reference) <ref name="ref2" />. (D) The distribution of CysR10 as visualized using anti-CysR10 and rhodamine-conjugated secondary antibodies. (E) The localization of CysP13 using anti-CysP13 and FITC-conjugated secondary antibodies. (F) Merged image of D and E. Bars in (D–F): 10mm..'']]
 Immunofluorescence light microscopy confirmed the spatial distribution of these prolamins within the PBs. CysR10 was visualized as small particles when labeled by anti-CysR10 followed by rhodamine-conjugated secondary antibodies (Fig. 1D). The distribution of CysR10 co-localized with CysP13, which was visualized with fluorescein isothiocyanate (FITC)-conjugated secondary antibodies (Fig. 1 E, F arrows). CysR10 was observed at the center of the PBs, whereas the distribution of CysP13 was more varied. Details about the spatial relationship between the prolamins were confirmed by immunofluorescence microscopy images from developing endosperm at 3 WAF (Fig. 2). They show that PB-I is composed of a center core of CysR10, surrounded by a middle layer of a mixture of CysR10 and CysP13, and then followed by a peripheral layer containing CysP13 devoid of CysR10. By immunoelectron microscopy, a more detailed structure of PB-I can be analyzed through its ultrastructure during different stages of seed development (at 5 DAF, 1 WAF, 2 WAF, and 3 WAF), then the Schematic images of PB-I structure during rice endosperm development can be obtained (Fig. 5).
 The prolamin-containing PB-Is were non-spherical in the CysR10-repressed endosperm, because CysR10 is required for forming PB-Is into the spherical shape and for the compact size, and that it not only forms the central core but also interacts with other Cys-rich prolamins to assemble the concentric ring structure within the PB-I. In addition, RNAi suppression of CysR10 slightly reduced the expression level of CysP13, but CysR16 and CysR14 were normal or slightly higher amounts. However, Kawakatsu ''et al.''<ref name="ref6" /> reported that their 10 kDa prolamin-suppressed plant accumulated substantially higher levels (about three times compared with the wild type) of CysR14 (RM1 and RM9) and CysR16 (RP16) prolamins than normal, although CysP13 (RM2 and RM4) prolamins were lower amounts. This different result may due to the differences of the methods used to regulate down the CysR10 expression level <ref name="ref7" />. One is the conventional RNAi method with the inverted CysR10 open reading frame, and the other one is the expression of a modified human Glucagon-like peptide-1 (GLP-1) to regulate down the target proteins. This elevated levels of CysR14 and CysR16 may compensate for the loss of CysR10 and contribute to form a rigid normal sized PB-I. Another consist result came from an endosperm storage protein mutant that contains reduced levels of CysR16, CysR14 and CysR10 and displays abnormal large PBIs.

@@ Line 8: / Line 8: @@
 ===Expression===
-[[File:.jpg|right|thumb|430px|'''Fig 1.''' ''Distribution of CysR10 and CysP13 in PB-Is of developing rice endosperm at 3 WAF (from reference) <ref name="ref2" />. (D) The distribution of CysR10 as visualized using anti-CysR10 and rhodamine-conjugated secondary antibodies. (E) The localization of CysP13 using anti-CysP13 and FITC-conjugated secondary antibodies. (F) Merged image of D and E. Bars in (D–F): 10mm..'']]
+[[File:Fig. 1.jpg|right|thumb|430px|'''Fig 1.''' ''Distribution of CysR10 and CysP13 in PB-Is of developing rice endosperm at 3 WAF (from reference) <ref name="ref2" />. (D) The distribution of CysR10 as visualized using anti-CysR10 and rhodamine-conjugated secondary antibodies. (E) The localization of CysP13 using anti-CysP13 and FITC-conjugated secondary antibodies. (F) Merged image of D and E. Bars in (D–F): 10mm..'']]
 Immunofluorescence light microscopy confirmed the spatial distribution of these prolamins within the PBs. CysR10 was visualized as small particles when labeled by anti-CysR10 followed by rhodamine-conjugated secondary antibodies (Fig. 1D). The distribution of CysR10 co-localized with CysP13, which was visualized with fluorescein isothiocyanate (FITC)-conjugated secondary antibodies (Fig. 1 E, F arrows). CysR10 was observed at the center of the PBs, whereas the distribution of CysP13 was more varied. Details about the spatial relationship between the prolamins were confirmed by immunofluorescence microscopy images from developing endosperm at 3 WAF (Fig. 2). They show that PB-I is composed of a center core of CysR10, surrounded by a middle layer of a mixture of CysR10 and CysP13, and then followed by a peripheral layer containing CysP13 devoid of CysR10. By immunoelectron microscopy, a more detailed structure of PB-I can be analyzed through its ultrastructure during different stages of seed development (at 5 DAF, 1 WAF, 2 WAF, and 3 WAF), then the Schematic images of PB-I structure during rice endosperm development can be obtained (Fig. 5).
 The prolamin-containing PB-Is were non-spherical in the CysR10-repressed endosperm, because CysR10 is required for forming PB-Is into the spherical shape and for the compact size, and that it not only forms the central core but also interacts with other Cys-rich prolamins to assemble the concentric ring structure within the PB-I. In addition, RNAi suppression of CysR10 slightly reduced the expression level of CysP13, but CysR16 and CysR14 were normal or slightly higher amounts. However, Kawakatsu ''et al.''<ref name="ref6" /> reported that their 10 kDa prolamin-suppressed plant accumulated substantially higher levels (about three times compared with the wild type) of CysR14 (RM1 and RM9) and CysR16 (RP16) prolamins than normal, although CysP13 (RM2 and RM4) prolamins were lower amounts. This different result may due to the differences of the methods used to regulate down the CysR10 expression level <ref name="ref7" />. One is the conventional RNAi method with the inverted CysR10 open reading frame, and the other one is the expression of a modified human Glucagon-like peptide-1 (GLP-1) to regulate down the target proteins. This elevated levels of CysR14 and CysR16 may compensate for the loss of CysR10 and contribute to form a rigid normal sized PB-I. Another consist result came from an endosperm storage protein mutant that contains reduced levels of CysR16, CysR14 and CysR10 and displays abnormal large PBIs.

← Older revision		Revision as of 08:08, 4 June 2014
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	The prolamin-containing PB-Is were non-spherical in the CysR10-repressed endosperm, because CysR10 is required for forming PB-Is into the spherical shape and for the compact size, and that it not only forms the central core but also interacts with other Cys-rich prolamins to assemble the concentric ring structure within the PB-I. In addition, RNAi suppression of CysR10 slightly reduced the expression level of CysP13, but CysR16 and CysR14 were normal or slightly higher amounts. However, Kawakatsu ''et al.''<ref name="ref6" /> reported that their 10 kDa prolamin-suppressed plant accumulated substantially higher levels (about three times compared with the wild type) of CysR14 (RM1 and RM9) and CysR16 (RP16) prolamins than normal, although CysP13 (RM2 and RM4) prolamins were lower amounts. This different result may due to the differences of the methods used to regulate down the CysR10 expression level <ref name="ref7" />. One is the conventional RNAi method with the inverted CysR10 open reading frame, and the other one is the expression of a modified human Glucagon-like peptide-1 (GLP-1) to regulate down the target proteins. This elevated levels of CysR14 and CysR16 may compensate for the loss of CysR10 and contribute to form a rigid normal sized PB-I. Another consist result came from an endosperm storage protein mutant that contains reduced levels of CysR16, CysR14 and CysR10 and displays abnormal large PBIs.		The prolamin-containing PB-Is were non-spherical in the CysR10-repressed endosperm, because CysR10 is required for forming PB-Is into the spherical shape and for the compact size, and that it not only forms the central core but also interacts with other Cys-rich prolamins to assemble the concentric ring structure within the PB-I. In addition, RNAi suppression of CysR10 slightly reduced the expression level of CysP13, but CysR16 and CysR14 were normal or slightly higher amounts. However, Kawakatsu ''et al.''<ref name="ref6" /> reported that their 10 kDa prolamin-suppressed plant accumulated substantially higher levels (about three times compared with the wild type) of CysR14 (RM1 and RM9) and CysR16 (RP16) prolamins than normal, although CysP13 (RM2 and RM4) prolamins were lower amounts. This different result may due to the differences of the methods used to regulate down the CysR10 expression level <ref name="ref7" />. One is the conventional RNAi method with the inverted CysR10 open reading frame, and the other one is the expression of a modified human Glucagon-like peptide-1 (GLP-1) to regulate down the target proteins. This elevated levels of CysR14 and CysR16 may compensate for the loss of CysR10 and contribute to form a rigid normal sized PB-I. Another consist result came from an endosperm storage protein mutant that contains reduced levels of CysR16, CysR14 and CysR10 and displays abnormal large PBIs.
		+
		+	Protein disulfide isomerase (PDI) family oxidoreductase PDIL2;3 knockdown inhibited the accumulation of Cys-rich 10-kD prolamin (crP10) in the core of PB-I. Conversely, crP10 (CysR10) knockdown dispersed PDIL2;3 into the endoplasmic reticulum lumen <ref name="ref3" />.

	===Evolution===		===Evolution===

← Older revision		Revision as of 07:21, 4 June 2014
Line 8:		Line 8:

	===Expression===		===Expression===
		+	[[File:Fig_1.jpg\|right\|thumb\|430px\|'''Fig 1.''' ''Distribution of CysR10 and CysP13 in PB-Is of developing rice endosperm at 3 WAF (from reference) <ref name="ref2" />. (D) The distribution of CysR10 as visualized using anti-CysR10 and rhodamine-conjugated secondary antibodies. (E) The localization of CysP13 using anti-CysP13 and FITC-conjugated secondary antibodies. (F) Merged image of D and E. Bars in (D–F): 10mm..'']]
	Immunofluorescence light microscopy confirmed the spatial distribution of these prolamins within the PBs. CysR10 was visualized as small particles when labeled by anti-CysR10 followed by rhodamine-conjugated secondary antibodies (Fig. 1D). The distribution of CysR10 co-localized with CysP13, which was visualized with fluorescein isothiocyanate (FITC)-conjugated secondary antibodies (Fig. 1 E, F arrows). CysR10 was observed at the center of the PBs, whereas the distribution of CysP13 was more varied. Details about the spatial relationship between the prolamins were confirmed by immunofluorescence microscopy images from developing endosperm at 3 WAF (Fig. 2). They show that PB-I is composed of a center core of CysR10, surrounded by a middle layer of a mixture of CysR10 and CysP13, and then followed by a peripheral layer containing CysP13 devoid of CysR10. By immunoelectron microscopy, a more detailed structure of PB-I can be analyzed through its ultrastructure during different stages of seed development (at 5 DAF, 1 WAF, 2 WAF, and 3 WAF), then the Schematic images of PB-I structure during rice endosperm development can be obtained (Fig. 5).		Immunofluorescence light microscopy confirmed the spatial distribution of these prolamins within the PBs. CysR10 was visualized as small particles when labeled by anti-CysR10 followed by rhodamine-conjugated secondary antibodies (Fig. 1D). The distribution of CysR10 co-localized with CysP13, which was visualized with fluorescein isothiocyanate (FITC)-conjugated secondary antibodies (Fig. 1 E, F arrows). CysR10 was observed at the center of the PBs, whereas the distribution of CysP13 was more varied. Details about the spatial relationship between the prolamins were confirmed by immunofluorescence microscopy images from developing endosperm at 3 WAF (Fig. 2). They show that PB-I is composed of a center core of CysR10, surrounded by a middle layer of a mixture of CysR10 and CysP13, and then followed by a peripheral layer containing CysP13 devoid of CysR10. By immunoelectron microscopy, a more detailed structure of PB-I can be analyzed through its ultrastructure during different stages of seed development (at 5 DAF, 1 WAF, 2 WAF, and 3 WAF), then the Schematic images of PB-I structure during rice endosperm development can be obtained (Fig. 5).

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 ==Labs working on this gene==
-Please input related labs here.
+Institute of Genetic Resources, Faculty of Agriculture, Kyushu University, Japan
 ==References==