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Accumulation of Soybean Glycinin and Its Assembly with the Glutelins in Rice1

Tomoyuki Katsube, Nobuyuki Kurisaka, Masahiro Ogawa, Nobuyuki Maruyama, Reiko Ohtsuka, Shigeru Utsumi2, *, and Fumio Takaiwa2

Research Institute for Food Science, Kyoto University, Uji, Kyoto 611-0011, Japan (T.K., N.M., S.U.); Shimane Women's College, Matsue, Shimane 690-0044, Japan (T.K.); Ehime Prefectural Agricultural Experiment Station, Houjo, Ehime 799-2424, Japan (N.K.); Yamaguchi Prefectural University, Department of Domestic Economy, Sakurabatake, Yamaguchi 753-8502, Japan (M.O.); Faculty of Agriculture, Kyushu University, Hakozaki, Higashiku, Fukuoka 812-8581, Japan (R.O.); and National Institute of Agrobiological Resources, Tsukuba, Ibaraki 305-0856, Japan (F.T.)

Saline-soluble glycinins and insoluble glutelins are the major storage proteins in soybean (Glycine max) and rice (Oryza sativa), respectively. In spite of their differences in solubility properties, both proteins are members of the 11S globulin gene family based on their similarities in primary sequences and processing of the coded protein. Wild-type and methionine-modified glycinin coding sequences were expressed in transgenic rice plants under the control of the rice glutelin GluB-1 promoter. Glycinins were specifically synthesized in the endosperm tissue and co-localized with glutelins in type II protein bodies. They assembled into 7S and 11S species, similar to what was observed in developing soybean seeds. This pattern was quite different from that displayed by the rice glutelins in untransformed plants, in which processed subunits sedimenting at 2S were apparent. In glycinin-expressing transgenic plants, however, glutelins were observed sedimenting at 7S and 11S with lesser amounts in the 2S region. A portion of the glycinins was also found associated in the insoluble glutelin fraction. Renaturation experiments suggested that the hybrid glycinin-glutelin oligomers were formed through specific interactions. Overall, these results indicate that despite significant differences in the assembly of soybean glycinin and rice glutelin, both proteins can assemble with each other to form soluble hexameric oligomers or insoluble aggregates.

1   This work was supported in part by grants from the Program for Promotion of Basic Research Activities for Innovative Biosciences (to S.U. and F.T.), the Ministry of Agriculture, Forestry, and Fisheries of Japan (to T.K., S.U., and F.T.), and Takano Life Science Research Foundation (to S.U.).
2   These authors contributed equally to the paper.
*   Corresponding author; e-mail utsumi{at}soya.food.kyoto-u.ac.jp; fax 81-774-38-3761.

Plant Physiol. (1999) 120: 1063-1074
Copyright Clearance Center:   0032-0889/99/120//12
© 1999 American Society of Plant Physiologists




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