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JXB Advance Access published online on June 15, 2009
Journal of Experimental Botany, doi:10.1093/jxb/erp187
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© 2009 The Author(s).
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. This paper is available online free of all access charges (see http://jxb.oxfordjournals.org/open_access.html for further details)

RESEARCH PAPER

Expression of unprocessed glutelin precursor alters polymerization without affecting trafficking and accumulation

Yuhya Wakasa, Lijun Yang, Sakiko Hirose and Fumio Takaiwa*

Transgenic Crop Research and Development Center, National Institute of Agrobiological Sciences, Kannondai 3-1-3, Tsukuba, Ibaraki 305-8604, Japan

* To whom correspondence should be addressed. E-mail: takaiwa{at}nias.affrc.go.jp

Rice glutelin is synthesized as a precursor in the endosperm endoplasmic reticulum and then deposited within the protein storage vacuole protein body-II (PB-II) as an aggregate, with a high degree of polymerized higher-order structure comprising mature acidic and basic subunits after post-translation processing cleavage. In order to investigate the functional role of this processing and its effect on folding assembly, wild-type GluA2 and its mutant cDNA (mGluA2), in which the conserved processing site (Asn-Gly) at the junction between the acidic and basic chains was replaced with Ala-Ala, were expressed under the control of the endosperm-specific GluB1 promoter in the mutant rice a123 line lacking glutelin GluA1, GluA2, and GluB4. The mGluA2 precursor was synthesized and stably targeted to PB-II without processing in the transgenic rice seeds like the wild-type GluA2. Notably, the saline-soluble mGluA2 precursor assembled with the other type of processed glutelin GluB as a trimer in PB-II, although such hetero-assembly with GluB was not detected in the transformant containing the processed GluA. Furthermore, the mGluA2 precursor in the glutelin fraction was deposited in PB-II by forming a quite different complex from the processed mature GluA2 products. These results indicate that post-translational processing of glutelin is not necessary for trafficking and stable accumulation in PB-II, but is required for the formation of the higher-order structure required for stacking in PB-II.

Key words: assembly, glutelin, glutelin mutant, Oryza sativa L., processing

Received 3 February 2009; Revised 22 April 2009 Accepted 14 May 2009


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