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Science 12 November 1993:
Vol. 262. no. 5136, pp. 1054 - 1056
DOI: 10.1126/science.8235623
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Articles

Science, Vol 262, Issue 5136, 1054-1056
Copyright © 1993 by American Association for the Advancement of Science

articles

Rice prolamine protein body biogenesis: a BiP-mediated process

X Li, Y Wu, DZ Zhang, JW Gillikin, RS Boston, VR Franceschi, and TW Okita

Department of Genetics and Cell Biology, Washington State University, Pullman 99164.

Rice prolamines are sequestered within the endoplasmic reticulum (ER) lumen even though they lack a lumenal retention signal. Immunochemical and biochemical data show that BiP, a protein that binds lumenal polypeptides, is localized on the surface of the aggregated prolamine protein bodies (PBs). BiP also forms complexes with nascent chains of prolamines in polyribosomes and with free prolamines with distinct adenosine triphosphate sensitivities. Thus, BiP retains prolamines in the lumen by facilitating their folding and assembly into PBs.


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