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


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1983-05

AUTHORS

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

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. More... »

PAGES

119-127

Journal

TITLE

Plant Molecular Biology

ISSUE

3

VOLUME

2

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf01578512

DOI

http://dx.doi.org/10.1007/bf01578512

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1035031007

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/24318206


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