Comparison of the primary structure of waxy proteins (granule-bound starch synthase) between polyploid wheats and related diploid species.

The waxy proteins encoded by the genomes A, B, and D in polyploid wheats and related diploid species were isolated by SDS-PAGE. The N-terminal amino acid sequences of mature proteins and V8 protease-induced fragments were determined. A total of five amino acid substitutions was detected in these sequences, which represent about 10% of the whole sequences of the waxy proteins. A comparison of these sequences in polyploid wheats with those in related diploid species revealed the following: (i) waxy proteins encoded by the A genome of polyploid wheats were identical to that of Triticum monococcum, (ii) the waxy protein encoded by the B genome of T. turgidum was identical to that of T. searsii, but differed from those of T. speltoides and T. longissimum by one amino acid substitution, (iii) the waxy protein encoded by the B genome of T. aestivum differed from that encoded by the B genome of T. turgidum by one amino acid substitution, and (iv) the waxy protein encoded by the D genome of T. aestivum was identical to that of T. tauschii.