| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1952272 | Biochimie | 2011 | 9 Pages |
To detect proteins binding to CUG triplet repeats, we performed magnetic bead affinity assays and North-Western analysis using a (CUG)10 ssRNA probe and either nuclear or total extracts from rat L6 myoblasts. We report the isolation and identification by mass spectrometry and immunodetection of α-enolase, as a novel (CUG)n triplet repeat binding protein. To confirm our findings, rat recombinant α-enolase was cloned, expressed and purified; the RNA binding activity was verified by electrophoretic mobility shift assays using radiolabeled RNA probes. Enolase may play other roles in addition to its well described function in glycolysis.
► α-enolase binds to RNA. ► α-enolase binding activity does not require additional factors. ► Recombinant α-enolase binds to RNA with a Kd = 4.9 μM.
