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Correct post-translational modification and stable vacuolar accumulation of phytohemagglutinin engineered to contain
S Kjemtrup1, E M Herman, M J Chrispeels
1Department of Biology, University of California, San Diego 92093-0116.
European Journal of Biochemistry
|December 1, 1994
Abstract:
Most legume seed storage proteins are deficient in sulfur amino acids. In this study, we demonstrate that replacing specific amino acid residues of a seed protein with methionine residues at positions known to be occupied by methionine residues in homologous proteins, is an effective strategy to create methionine-enriched seed proteins. Mutant phytohemagglutinin polypeptides with three or four methionine residues were found to undergo correct post-translational modifications in transformed cultured tobacco cells and to accumulate stably in the protein storage vacuoles of transgenic tobacco seeds.