Pollen proteins after two-dimensional gel electrophoresis and pollen morphology of the amphiploids Aegilops kotschyi and Ae. variabilis with Secale cereale

Proteins from pollen of parent forms and amphiploids Aegilops variabilis x Secale cereale and Ae. kotschyi x S. cereale, obtained by in vitro propagat ion or colchicine treatment of F-1 hybrids, were subjected to a study by tw o-dimensional (2-D) electrophoresis. Qualitative and quantitative diversiti es of protein patterns were revealed for the amphiploid pollen. The majorit y of peptides found in the parent forms were also present in the patterns o f the amphiploid pollen; however, some of the parent-form-peptides were not expressed and proteins characteristic only of the amphiploids appeared. In the 2-D combined protein pattern obtained for the parent forms, amphiploid s Ac. variabilis x S. cereale produced pollen with a poorer spectrum of pro teins. In amphiploid 408B, obtained from treated the F-1 generation with co lchicine, the 2-D pattern revealed the presence of less than 50% of the pro teins recorded for the parent forms. Pollen grain morphology was studied un der a scanning microscope. The structure and shape of exines differed from those of the parents. In the parent forms the pollen grains had only one po re, while in amphiploid pollen, one, two or three pores were observed. Poss ible explanations for the differences in the 2-D patterns of amphiploids an d their parent forms (impoverishment of the protein spectrum and appearance of new peptides) are (1) somaclonal variation and mutagenic activity of co lchicine, (2) suppression of structural genes, (3) activity of regulators a nd (4) translocations. Pollen grains with two or even three pores could app ear as a result of the independent activity of the genes from three amphipl oidal genomes.