Germ cell-specific proteins interact with the 3' untranslated regions of Prm-1 and Prm-2 mRNA

A comparison of the translational capacity of deproteinized Prm-1 mRNA extracted in an in vitro translation system from elongating and round spermatid populations reveals comparable translation efficiencies in wheat germ extracts of Prm-1 mRNAs from both spermatids, indicating the competence of Prm-1 signal in round spermatids for translation. An RNA band shift assay helps delineate an activity in meiotic spermatocyte and postmeiotic round spermatid cytoplasm, which associates with the 3'UTRs of Prm-2 and Prm-1 mRNA. The binding site is present at the 22-nt region in the Prm-1 3'UTR and at the 20-nt region in the Prm-2 3'UTR. The 3'UTRs of Prm-1 and Prm-2 mRNAs associate sequence-specifically with two germ cell proteins of 50 and 48 kDa.