Effect of structural modifications on the assembly of a glycinin subunit

A Gy4 glycinin cDNA was modified and used to produce structurally altered 11S storage protein subunits. We evaluated these modified subunits for their ability to assemble into oligomers. Alterations made in the acidic polypeptide changed the subunit solubility characteristics but did not eliminate a...

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Bibliographic Details
Published in:The Plant cell 1990-05, Vol.2 (5), p.403-413
Main Authors: Dickinson, C.D. (University of California, La Jolla, CA), Scott, M.P, Hussein, E.H.A, Argos, P, Nielson, N.C
Format: Article
Language:English
Subjects:
Amino acids
Base Sequence
DNA
DNA Mutational Analysis
GENE
GENES
Genes, Plant - genetics
Globulins - genetics
Globulins - metabolism
GLYCINE MAX
Glycine max - genetics
Glycine max - metabolism
GRAINE
Macromolecular Substances
Models, Biological
Molecular Sequence Data
Monomers
MUTACION
MUTATION
Oligomers
Plant cells
Plant Proteins, Dietary - genetics
Plant Proteins, Dietary - metabolism
Plasmids
POLIMERIZACION
POLYMERISATION
Protein Precursors - metabolism
Protein Structure, Tertiary
PROTEINAS VEGETALES
PROTEINE VEGETALE
Proteins
Self assembly
SEMILLA
SINTESIS DE PROTEINAS
Soybean Proteins
Soybeans
SYNTHESE PROTEIQUE
Trimers
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Summary:A Gy4 glycinin cDNA was modified and used to produce structurally altered 11S storage protein subunits. We evaluated these modified subunits for their ability to assemble into oligomers. Alterations made in the acidic polypeptide changed the subunit solubility characteristics but did not eliminate assembly. Modifications in the basic polypeptide usually eliminated assembly of subunits into trimers. A region exhibiting high natural variability located at the COOH terminus of the acidic polypeptide that we have designated the hypervariable region was also studied. Extensive deletions and insertions were tolerated in the hypervariable region without perturbing subunit assembly. Some of the insertions significantly increased the methionine content in the Gy4 glycinin subunit. Together, our results indicated that the structure of the basic polypeptide was more critical for assembly of trimers than that of the acidic polypeptide, an observation that implies that the basic polypeptides direct trimer formation. The assembly assays described here will be useful in efforts to improve seed quality. Using them, the effects of modifications to the storage protein subunits can be rapidly evaluated before introducing the mutated genes into plants
ISSN:1040-4651
1532-298X
DOI:10.1105/tpc.2.5.403