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Biochimie. 2011 Sep;93(9):1520-8. doi: 10.1016/j.biochi.2011.05.007. Epub 2011 May 20.

α-Enolase binds to RNA.

Author information

1
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.

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.

PMID:
21621582
DOI:
10.1016/j.biochi.2011.05.007
[Indexed for MEDLINE]

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