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Plant Cell, Vol. 10, 343-358, Copyright © 1998, American Society of Plant Physiologists

The Role of Proteolysis in the Processing and Assembly of 11S Seed Globulins

Rudolf Junga,b, M. Paul Scotta, Young-Woo Nama, Todd W. Beamana, Ronald Bassünera, Isolde Saalbachb, Klaus Müntzb, and Niels C. Nielsena
a United States Department of Agriculture–Agricultural Research Service and the Departments of Agronomy and Biochemistry, Purdue University, West Lafayette, Indiana 47907
b Institute of Plant Genetics and Crop Plant Research, Corrensstrasse 3, D-06466 Gatersleben, Germany

Correspondence to: Niels C. Nielsen, nnielsen{at}dept.agry.purdue.edu (E-mail), 765-494-6508 (fax).

11S seed storage proteins are synthesized as precursors that are cleaved post-translationally in storage vacuoles by an asparaginyl endopeptidase. To study the specificity of the reaction catalyzed by this asparaginyl endopeptidase, we prepared a series of octapeptides and mutant legumin B and G4 glycinin subunits. These contained amino acid mutations in the region surrounding the cleavage site. The endopeptidase had an absolute specificity for Asn on the N-terminal side of the severed peptide bond but exhibited little specificity for amino acids on the C-terminal side. The ability of unmodified and modified subunits to assemble into hexamers after post-translational modification was evaluated. Cleavage of subunits in trimers is required for hexamer assembly in vitro. Products from a mutant gene encoding a noncleavable prolegumin subunit (LeB{Delta}N281) accumulated as trimers in seed of transgenic tobacco, but products from the unmodified prolegumin B gene accumulated as hexamers. Therefore, the asparaginyl endopeptidase is required for hexamer assembly.




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