Correct Post‐Translational Modification and Stable Vacuolar Accumulation of Phytohemagglutinin Engineered to Contain Multiple Methionine Residues

Susanne Kjemtrup, Eliot M. Herman, Maarten J. Chrispeels

Research output: Contribution to journalArticle

9 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)385-391
Number of pages7
JournalEuropean Journal of Biochemistry
Volume226
Issue number2
DOIs
StatePublished - Dec 1994
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry

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