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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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