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- W4306173651 abstract "Estrogen receptor alpha (ERα) is a ligand-responsive transcription factor critical for sex determination and development. Recent reports challenge the canonical view of ERα function by suggesting an activity beyond binding dsDNA at estrogen-responsive promotor elements: association with RNAs in vivo. Whether these interactions are direct or indirect remains unknown, which limits the ability to understand the extent, specificity, and biological role of ERα-RNA binding. Here we demonstrate that an extended DNA-binding domain of ERα directly binds a wide range of RNAs in vitro with structural specificity. ERα binds RNAs that adopt a range of hairpin-derived structures independent of sequence, while interacting poorly with single- and double-stranded RNA. RNA affinities are only 4-fold weaker than consensus dsDNA and significantly tighter than nonconsensus dsDNA sequences. Moreover, RNA binding is competitive with DNA binding. Together, these data show that ERα utilizes an extended DNA-binding domain to achieve a high-affinity/low-specificity mode for interacting with RNA." @default.
- W4306173651 created "2022-10-14" @default.
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- W4306173651 date "2022-10-14" @default.
- W4306173651 modified "2023-10-03" @default.
- W4306173651 title "An Extended DNA Binding Domain of the Estrogen Receptor Alpha Directly Interacts with RNAs <i>in Vitro</i>" @default.
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- W4306173651 doi "https://doi.org/10.1021/acs.biochem.2c00536" @default.
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