Nucleotide homologies between the glycosylated seed storage proteins ofGlycine max andPhaseolus vulgaris

Abstract

We have compared the partial nucleotide and derived amino acid sequences of a phaseolin seed storage protein gene ofPhaseolus vulgaris (1) and a conglycinin storage protein gene ofGlycine max (2). Although these proteins are not antigenically related to one another, the architecture of the genes is similar throughout the sequences compared here. Intervening sequences interrupt the same amino acid positions in both genes. Within the 28% of theG. max gene and the 38% of theP. vulgaris gene represented in this comparison, 73% of the nucleotides in the coding and intervening sequences are identical, excluding the insertions and deletions. The nucleotide mismatches found in the coding sequences are distributed throughout the three codon positions with little bias towards the third codon position. In addition to the single nucleotide differences, six insertions or deletions, ranging from three to twenty-seven nucleotides in length, occur in this portion of the coding region and these are partially responsible for the molecular weight differences of the conglycinin α′-subunit and the phaseolin subunit.

DOI: 10.1007/BF01578512

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@article{Schuler1983NucleotideHB, title={Nucleotide homologies between the glycosylated seed storage proteins ofGlycine max andPhaseolus vulgaris}, author={Mary A. Schuler and Jeffrey J. Doyle and Roger N. Beachy}, journal={Plant Molecular Biology}, year={1983}, volume={2}, pages={119-127} }