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Plant and Cell Physiology Advance Access published online on September 6, 2008
Plant and Cell Physiology, doi:10.1093/pcp/pcn135
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© The Author 2008. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

Co-expression of soybean glycinins A1aB1b and A3B4 enhances their accumulation levels in transgenic rice seed

Fumio Takaiwa1,*, Chiyoko Sakuta1, Seon-Kang Choi2, Hirofumi Tada1, Takayasu Motoyama2 and Shigeru Utsumi2

1Transgenic Crop Research and Development Center, National Institute of Agrobiological Sciences, Kannondai 2-1-2, Tsukuba, Ibaraki 305-8602, Ibaraki
2Laboratory of Food Quality Design and Development, Graduate School of Agriculture, Kyoto University, Gokasho, Uji, Kyoto 611-0011, 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;+81-29-838-8373, E-mail: takaiwa{at}nisa.affrc.go.jp


  Abstract

The soybean major storage protein glycinin is encoded by five genes, which are divided into two subfamilies. Expression of A3B4 glycinin in transgenic rice seed reached about 1.5% of total seed protein, even if expressed under the control of strong endosperm-specific promoters. In contrast, expression of A1aB1b glycinin reached about 4% of total seed protein. Co-expression of the two proteins doubled accumulation levels of both A1aB1b and A3B4 glycinins. This increase can be largely accounted for by their aggregation with rice glutelins, self-assembly, and inter-glycinin interactions, resulting in the enrichment of globulin and glutelin fractions and a concomitant reduction of the prolamin fraction. Immunoelectron-microscopy indicated that the synthesized A1aB1b glycinin was predominantly deposited in protein body-II storage vacuoles (PB-II), whereas A3B4 glycinin is targeted to both PB-II and endoplasmic reticulum (ER) derived protein body-I storage structures (PB-I). Co-expression with A1aB1b facilitated targeting of A3B4 glycinin into PB-II by sequestration with A1aB1b, resulting in an increase in the accumulation of A3B4 glycinin.

Keywords: Endosperm - Immunolocalization - Gycinin - Protein body - Seed storage protein - Transgenic rice

(Received June 22, 2008; Accepted August 29, 2008)
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