Male germ cell extracts contain proteins binding to the conserved 3'-end of mouse p68 RNA helicase mRNA.

The 3'-untranslated regions of human and mouse p68 RNA helicase mRNA are highly conserved, suggesting a functional role of the nucleic acid sequence itself in regulation of p68 RNA helicase expression. Secondary structure evaluations revealed no indications for a predominant folding pattern within the 3'-UTR. To test the potential of the 3'-sequence to serve as a target for specific binding proteins, gel shift assays were performed. In vitro-synthesized RNA was incubated with cytoplasmic as well as nuclear extracts from mouse male germ cells. Evidence was obtained that such specific proteins exist in germ cell extracts. Photo-crosslinking experiments suggested that a 30 kDa protein was involved in these binding events.