Os03g0758100
Plastidial phosphorylase (Pho1) accounts for ~96% of the total phosphorylase activity in developing rice (Oryza sativa) seeds.
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Annotated Information
Function
Mutation
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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[1].
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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. [2].
Expression
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Evolution
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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
- ↑ 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.
- ↑ 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.
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