RNA Helicase Associated with AU-rich Element (RHAU/DHX36) Interacts with the 3'-Tail of the Long Non-coding RNA BC200 (BCYRN1)
| Autor: | Ewan K.S. McRae, Jörg Stetefeld, Edis Dzananovic, Markus Meier, Ryan Howard, Sean A. McKenna, Soumya Deo, Emmanuel O. Ariyo, Evan P. Booy |
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| Rok vydání: | 2015 |
| Předmět: |
0301 basic medicine
RNase P Molecular Sequence Data Biology Biochemistry DEAD-box RNA Helicases 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine DHX36 RNA-Protein Interaction Humans heterocyclic compounds Nucleic acid structure Molecular Biology Binding Sites Base Sequence C-terminus RNA Cell Biology Molecular biology RNA Helicase A Cell biology G-Quadruplexes 030104 developmental biology HEK293 Cells chemistry MCF-7 Cells RNA Long Noncoding 030217 neurology & neurosurgery DNA HeLa Cells Protein Binding |
| Zdroj: | The Journal of biological chemistry. 291(10) |
| ISSN: | 1083-351X |
| Popis: | RNA helicase associated with AU-rich element (RHAU) is an ATP-dependent RNA helicase that demonstrates high affinity for quadruplex structures in DNA and RNA. To elucidate the significance of these quadruplex-RHAU interactions, we have performed RNA co-immunoprecipitation screens to identify novel RNAs bound to RHAU and characterize their function. In the course of this study, we have identified the non-coding RNA BC200 (BCYRN1) as specifically enriched upon RHAU immunoprecipitation. Although BC200 does not adopt a quadruplex structure and does not bind the quadruplex-interacting motif of RHAU, it has direct affinity for RHAU in vitro. Specifically designed BC200 truncations and RNase footprinting assays demonstrate that RHAU binds to an adenosine-rich region near the 3′-end of the RNA. RHAU truncations support binding that is dependent upon a region within the C terminus and is specific to RHAU isoform 1. Tests performed to assess whether BC200 interferes with RHAU helicase activity have demonstrated the ability of BC200 to act as an acceptor of unwound quadruplexes via a cytosine-rich region near the 3′-end of the RNA. Furthermore, an interaction between BC200 and the quadruplex-containing telomerase RNA was confirmed by pull-down assays of the endogenous RNAs. This leads to the possibility that RHAU may direct BC200 to bind and exert regulatory functions at quadruplex-containing RNA or DNA sequences. |
| Databáze: | OpenAIRE |
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