PMID: 8580763Jan 1, 1995Paper

Accumulation and proteolytic processing of vicilin deletion-mutant proteins in the leaf and seed of transgenic tobacco

Planta
A R KermodeT J Higgins

Abstract

Vicilin, a 7S globulin of Pisum sativum L. seed, accumulates in protein-storage vacuoles (protein bodies) of cotyledonary storage-parenchyma cells. The synthesis and proteolytic processing of various genetically engineered proteins within the leaf and seed of a heterologous (tobacco, Nicotiana tabacum L.) host was examined. A modified vicilin gene, in which the DNA sequence corresponding to the signal peptide was removed, resulted in a polypeptide of 50 kDa in the tobacco leaf and seed; none of the normal proteolytic cleavage products characteristic of expression of an unmodified vicilin gene were obtained. Likewise, no vacuolar accumulation of this mutant vicilin occurred in leaf protoplasts, which is also supportive of the predicted cytosolic localization for this protein. In-frame deletions were made within the region of the vicilin gene encoding the mature protein, to eliminate the N-terminal 28 and 121 amino acids and the C-terminal 69 residues, while maintaining an intact signal peptide. All of these "mature" deletion-mutant proteins were accumulated to only low levels in the host, but exhibited the predicted molecular weight and underwent some normal proteolytic processing in the seed. Mutant vicilin proteins having dele...Continue Reading

Citations

Apr 1, 1997·Current Opinion in Biotechnology·L Yuan, V C Knauf
Nov 22, 1997·The Plant Cell·E PedrazziniA Vitale
Jan 13, 2010·PloS One·Sara MonteiroRicardo B Ferreira
Dec 21, 2006·Plant Biotechnology Journal·Willa L DowningAllison R Kermode
Nov 26, 1999·The Plant Journal : for Cell and Molecular Biology·J P MarcusJ M Manners

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