Prolamin variation and evolution in Triticeae as recognized by monoclonal antibodies

Abstract

The isopropanol-soluble seed storage proteins, prolamins, were studied in 18 different genera of the tribe Triticeae by gel electrophoresis, Coomassie staining, and immunoblot assays. The monoclonal antibodies were originally raised against cultivated barley (Hordeum vulgare L.) hordein, and their reactions had been tested earlier on wild Hordeum species. The study showed that all the investigated Triticeae species produce prolamins and that structural similarities can be found throughout the tribe. The presence of the same antigenic sites in all the species indicates that the polypeptides contain well-conserved regions. They also indicate that the prolamins of the Triticeae species have a common evolutionary origin. In all the investigated species an antigenic site that is common to the B- and C-hordeins of barley was detected. Some of the reacting polypeptides also contained a site that is only present in the B-hordeins. The B-hordein specific site was found in all genera except Agropyron, Hordelymus, and Secale. This shows that although there are similarities between individual polypeptides, the composition of the various prolamin groups may vary between different genera. In the polyploid Elymus species different banding patterns were observed depending on what basic genomes were represented. The results suggest a direct correlation between the presence of a fast migrating polypeptide containing the B-hordein specific site and the presence of the H genome.