title: α-Enolase binds to RNA.
abstract: 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.
authors.affiliation: Departamento de Genética y Biología Molecular, Centro de Investigación y de Estudios Avanzados del IPN., Avenida Instituto Politécnico Nacional 2508, Apartado postal 14-740, DF CP 07360, Mexico.
authors.forename: Liliana
authors.initials: L
authors.lastname: Hernández-Pérez
authors.forename: Francisco
authors.initials: F
authors.lastname: Depardón
authors.forename: Fernando
authors.initials: F
authors.lastname: Fernández-Ramírez
authors.forename: Alejandra
authors.initials: A
authors.lastname: Sánchez-Trujillo
authors.forename: Rosa María
authors.initials: RM
authors.lastname: Bermúdez-Crúz
authors.forename: Lawrence
authors.initials: L
authors.lastname: Dangott
authors.forename: Cecilia
authors.initials: C
authors.lastname: Montañez
mesh_terms: D000818:Animals; D001665:Binding Sites; D002460:Cell Line; D002467:Cell Nucleus / Q000378:metabolism; D024202:Electrophoretic Mobility Shift Assay; D032446:Myoblasts / Q000201:enzymology; D010751:Phosphopyruvate Hydratase / Q000737:chemistry* / Q000378:metabolism; D012313:RNA / Q000737:chemistry* / Q000378:metabolism; D051381:Rats
chemical_list: D012313:RNA; D010751:Phosphopyruvate Hydratase