| First Author | Sandhu H | Year | 1995 |
| Journal | Biochem Biophys Res Commun | Volume | 214 |
| Issue | 2 | Pages | 632-8 |
| PubMed ID | 7677776 | Mgi Jnum | J:28973 |
| Mgi Id | MGI:76510 | Doi | 10.1006/bbrc.1995.2333 |
| Citation | Sandhu H, et al. (1995) Male germ cell extracts contain proteins binding to the conserved 3'-end of mouse p68 RNA helicase mRNA. Biochem Biophys Res Commun 214(2):632-8 |
| abstractText | 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. |
