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THE PLANT CELL, Vol 1, Issue 4 459-469, Copyright © 1989 by American Society of Plant Biologists
Role of Posttranslational Cleavage in Glycinin Assembly
C. D. Dickinson, EHA. Hussein and N. C. Nielsen
United States Department of Agriculture/Agricultural Research Service, Department of Agronomy, Purdue University, West Lafayette, Indiana 47907
Glycinin, like other 11S seed storage proteins, undergoes a complex series
of posttranslational events between the time proglycinin precursors are
synthesized in endoplasmic reticulum and the mature glycinin subunits are
deposited in vacuolar protein bodies. According to the current
understanding of this process, proglycinin subunits aggregate into trimers
in endoplasmic reticulum, and then the trimers move to the vacuolar protein
bodies where a protease cleaves them into acidic and basic polypeptide
chains. Stable glycinin hexamers, rather than trimers, are isolated from
mature seeds. We used a re-assembly assay in this study to demonstrate that
proteolytic cleavage of the proglycinin subunits is required for in vitro
assembly of glycinin oligomers beyond the trimer stage. The possibility
that the cleavage is a regulatory step and that it triggers the deposition
of 11S seed storage proteins as insoluble aggregates in vivo is considered.
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