The complete deduced amino acid sequences of legumin β-polypeptides from different genetic loci inPisum
✍ Scribed by Claire Domoney; Dick Barker; Rod Casey
- Publisher
- Springer
- Year
- 1986
- Tongue
- English
- Weight
- 546 KB
- Volume
- 7
- Category
- Article
- ISSN
- 0167-4412
No coin nor oath required. For personal study only.
✦ Synopsis
The deduced amino acid sequences of the/3-polypeptides of Pisum legumin from two loci on chromosome 1 were compared with one from a locus on chromosome 7. The chromosome 1-derived sequences were -80°70 identical, but each was only -50o70 homologous to the chromosome 7-derived sequence. Comparison of these sequences with those of homologous polypeptides from two other species of the Leguminoseae showed that the chromosome 1-derived Pisum sequences were more similar to legumin B than to legumin A from Vicia faba and were more closely related to group II than to group I glycinins from Glycine max. The converse was true for the chromosome 7-derived Pisum sequences. This suggests that divergence of legumin-like sequences predated speciation in these three members of the Leguminoseae.
Among the three Pisum sequence classes, a highly variable region was identified within the ~-polypeptide, just to the amino-terminal side of the or/3 processing site. This region varied considerably in length within the three classes of Pisum u-polypeptide sequence, a variation which far exceeded that which has previously been described for other legumins and glycinins. The chromosome 7-derived, and one of the chromosome 1-derived ot-polypeptide sequences contained different tandem repeats in this region.