Difference between revisions of "Os03g0758100"
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===Mutation=== | ===Mutation=== | ||
* Mature seeds of >1700 mutant lines generated by MNU treatments of the Kinmaze and Taichung 65 (T65) japonica rice cultivars were screened for Pho1 mutants by SDS-PAGE analysis. Many mutant lines were identified that lacked the 106-kD polypeptide completely (Figure 3A) but did not exhibit any significant alterations in the expression of the other major endosperm proteins when assessed by SDS-PAGE. The complete loss of Pho1 was verified by protein gel blot analysis using anti- Pho1 (Figure 3A). Native-PAGE/activity staining analysis also showed the absence of the Pho1 activity band in the mutant lines, while the activity levels of Pho2 were comparative to that of the wild type (Figure 3B), indicating that expression of Pho1 and Pho2 are regulated independently. | * Mature seeds of >1700 mutant lines generated by MNU treatments of the Kinmaze and Taichung 65 (T65) japonica rice cultivars were screened for Pho1 mutants by SDS-PAGE analysis. Many mutant lines were identified that lacked the 106-kD polypeptide completely (Figure 3A) but did not exhibit any significant alterations in the expression of the other major endosperm proteins when assessed by SDS-PAGE. The complete loss of Pho1 was verified by protein gel blot analysis using anti- Pho1 (Figure 3A). Native-PAGE/activity staining analysis also showed the absence of the Pho1 activity band in the mutant lines, while the activity levels of Pho2 were comparative to that of the wild type (Figure 3B), indicating that expression of Pho1 and Pho2 are regulated independently. | ||
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| + | [[File:Os03g0758100-2.png|center|thumb|400px|'''Figure 3. Effects of pho1 Mutation on Pho1 Content and Activity in Rice Endosperm and on Morphology of the Kernel.''' '' <ref name="ref1" />.'']] | ||
===Subcellular localization=== | ===Subcellular localization=== | ||
Revision as of 15:05, 10 August 2016
Plastidial phosphorylase (Pho1) accounts for ~96% of the total phosphorylase activity in developing rice (Oryza sativa) seeds.
Contents
Annotated Information
Function
Mutation
- Mature seeds of >1700 mutant lines generated by MNU treatments of the Kinmaze and Taichung 65 (T65) japonica rice cultivars were screened for Pho1 mutants by SDS-PAGE analysis. Many mutant lines were identified that lacked the 106-kD polypeptide completely (Figure 3A) but did not exhibit any significant alterations in the expression of the other major endosperm proteins when assessed by SDS-PAGE. The complete loss of Pho1 was verified by protein gel blot analysis using anti- Pho1 (Figure 3A). Native-PAGE/activity staining analysis also showed the absence of the Pho1 activity band in the mutant lines, while the activity levels of Pho2 were comparative to that of the wild type (Figure 3B), indicating that expression of Pho1 and Pho2 are regulated independently.
Figure 3. Effects of pho1 Mutation on Pho1 Content and Activity in Rice Endosperm and on Morphology of the Kernel. [1].
Subcellular localization
- Unlike the amyloplast resident marker enzymes BEI and BEIIb, which were detected in both the stroma and starch fractions or the starchlocalized GBSSI, only trace amounts of Pho1 were starch bound (Figure 2). Hence, Pho1 is restricted to the stromacompartment of the amyloplasts. A stroma location was also observed for maize endosperm Pho1[2].
Figure 2. Subcellular Localization of Pho1 in Developing Endosperm Cells of Rice. Total endosperm proteins and proteins associated with starch granules of mid-developing seeds were resolved by SDS-PAGE and then subjected to immunoblotting for Pho1, BEI, BEIIb, and GBSSI. ‘‘Endosperm’’ denotes the total proteins extracted from the endosperm of developing seeds. [1].
Expression
Please input expression information here.
Evolution
Please input evolution information here.
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Labs working on this gene
- Plant Genetic Resources, Institute of Genetic Resources, Faculty of Agriculture, Kyushu University, Fukuoka 812-8581, Japan
- Institute of Biological Chemistry, Washington State University, Pullman, Washington, 99164-6340
- Faculty of Bioresource Science, Akita Prefectural University, Akita 010-0195, Japan
References
- ↑ 1.0 1.1 Satoh H, Shibahara K, Tokunaga T, et al. Mutation of the plastidial α-glucan phosphorylase gene in rice affects the synthesis and structure of starch in the endosperm[J]. The Plant Cell, 2008, 20(7): 1833-1849.
- ↑ Yu, Y., Mu, H.H., Wassermanm, B.P., and Carman, G.M. (2001). Identification of the maize amyloplast stromal 112-kD protein as a plastidic starch phosphorylase. Plant Physiol. 125: 351–359.
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