Nucleotide homologies between the glycosylated seed storage proteins of Glycine max and Phaseolus vulgaris

Mary A Schuler, Jeffrey J. Doyle, Roger N. Beachy

Research output: Contribution to journalArticlepeer-review


We have compared the partial nucleotide and derived amino acid sequences of a phaseolin seed storage protein gene of Phaseolus vulgaris (1) and a conglycinin storage protein gene of Glycine 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 the G. max gene and the 38% of the P. 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.

Original languageEnglish (US)
Pages (from-to)119-127
Number of pages9
JournalPlant Molecular Biology
Issue number3
StatePublished - May 1983
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)


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