Messenger RNA targeting of rice seed storage proteins to specific ER subdomains

Sang-Bong Choi, Changlin Wang, Douglas G. Muench, Kenjirou Ozawa, Vincent R. Franceschi, Yujia Wu and Thomas W. Okita ()
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Sang-Bong Choi: Institute of Biological Chemistry
Changlin Wang: Institute of Biological Chemistry
Douglas G. Muench: Department of Biological Sciences University of Calgary
Kenjirou Ozawa: National Institute of Agrobiological Resources
Vincent R. Franceschi: Washington State University
Yujia Wu: Institute of Biological Chemistry
Thomas W. Okita: Institute of Biological Chemistry

Nature, 2000, vol. 407, issue 6805, 765-767

Abstract: Abstract Rice seeds, a rich reserve of starch and protein, are a major food source in many countries. Unlike the seeds of other plants, which typically accumulate one major type of storage protein, rice seeds use two major classes, prolamines and globulin-like glutelins. Both storage proteins are synthesized on the endoplasmic reticulum (ER) and translocated to the ER lumen, but are then sorted into separate intracellular compartments1,2. Prolamines are retained in the ER lumen as protein bodies whereas glutelins are transported and stored in protein storage vacuoles. Mechanisms responsible for the retention of prolamines within the ER lumen and their assembly into intracisternal inclusion granules are unknown, but the involvement of RNA localization has been suggested3. Here we show that the storage protein RNAs are localized to distinct ER membranes and that prolamine RNAs are targeted to the prolamine protein bodies by a mechanism based on RNA signal(s), a process that also requires a translation initiation codon. Our results indicate that the ER may be composed of subdomains that specialize in the synthesis of proteins directed to different compartments of the plant endomembrane system.

Date: 2000
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DOI: 10.1038/35037633

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