Plant and Cell Physiology Advance Access published online on June 29, 2009
Plant and Cell Physiology, doi:10.1093/pcp/pcp098
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Overexpression of BiP has inhibitory effects on the accumulation of seed storage proteins in endosperm cells of rice
1 Transgenic Crop Research and Development Center, National Institute of Agrobiological Sciences, Kannondai 2-1-2, Tsukuba, Ibaraki 305-8602, Japan
2 Research Team for Crop Cold Tolerance, National Agricultural Research Center for Hokkaido region, Hitsujigaoka 1, Toyohira-ku, Sapporo, Hokkaido 062-8555, Japan
3 Rice Biotechnology Research Team, National Institute of Crop Sciences, Kannondai 2-1-18, Tsukuba, Ibaraki 305-8518, Japan
*Corresponding author: Dr. Fumio Takaiwa, Transgenic Crop Research and Development Center, National Institute of Agrobiological Sciences, Kannondai 2-1-2, Tsukuba, Ibaraki 305-8602, Ibaraki, Fax;+81-29-838-8397, E-mail: takaiwa{at}nias.affrc.go.jp
| Abstract |
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Seed storage proteins are specifically and highly synthesized during seed maturation and are deposited into protein bodies via the ER lumen. The accumulation process is mediated by ER chaperones such as BiP and PDI. To examine the role of ER chaperones and the relationship between ER chaperones and accumulation levels of seed storage proteins, we generated transgenic rice plants in which the rice BiP and PDI genes were overexpressed in an endosperm-specific manner under the control of the rice seed storage protein glutelin promoter. The seed phenotype of the PDI-overexpressing transformant was almost identical with that of the wild type, whereas overexpression of BiP resulted in transgenic rice seed that displayed an opaque phenotype with floury and shrunken features. In the BiP-overexpressing line, the accumulation levels of seed storage proteins and starch contents were significantly lower compared with wild type. Interestingly, overproduction of BiP in the endosperm of the transformant not only altered the morphological structure of ER-derived PB-I, but also generated unusual new protein body (PB)-like structures composed of a high-electron density matrix containing glutelin and BiP and a low-electron density matrix containing prolamins. Notably, polysomes were attached around the aberrant PB-like structures, indicating that this aberrant structure is an ER-derived PB-I derivative. These results suggested that the PB-like structure may be formed in the ER lumen, resulting in inhibition of translation, folding and transport of seed proteins.
Keywords: BiP - Chaperone proteins - ER stress - PB - PDI - Quality control - Storage proteins
(Received May 22, 2009; Accepted June 25, 2009)
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