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. 1998 Mar;10(3):343–357. doi: 10.1105/tpc.10.3.343

The role of proteolysis in the processing and assembly of 11S seed globulins.

R Jung 1, M P Scott 1, Y W Nam 1, T W Beaman 1, R Bassüner 1, I Saalbach 1, K Müntz 1, N C Nielsen 1
PMCID: PMC144002  PMID: 9501109

Abstract

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 (LeBDeltaN281) 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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Selected References

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