MALE GERM-CELL EXTRACTS CONTAIN PROTEINS BINDING TO THE CONSERVED 3'-END OF MOUSE P68 RNA HELICASE MESSENGER-RNA

The 3'-untranslated regions of human and mouse p68 RNA helicase mRNA a re highly consented, suggesting a functional role of the nucleic acid sequence itself in regulation of p68 RNA helicase expression. Secondar y structure evaluations revealed no indications for a predominant fold ing pattern within the 3'-UTR. To test the potential of the 3'-sequenc e to serve as a target for specific binding proteins, gel shift assays were performed. in vitro-synthesized RNA was incubated with cytoplasm ic as well as nuclear extracts from mouse male germ cells. Evidence wa s obtained that such specific proteins exist in Berm cell extracts; Ph oto-crosslinking, experiments suggested that a 30 kDa protein was invo lved in these binding events. (C) 1995 Academic Press Inc.