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• W2146372143 abstract "Determining the composition of messenger ribonucleoprotein (mRNP) particles is essential for a comprehensive understanding of the complex mechanisms underlying mRNA regulation, but is technically challenging. Here we present an RNA-based method to identify RNP components using a modified streptavidin (SA)-binding RNA aptamer termed S1m. By optimizing the RNA aptamer S1 in structure and repeat conformation, we improved its affinity for SA and found a 4-fold repeat of S1m (4×S1m) to be more efficient than the established MS2 and PP7 systems from bacteriophages. We then attached the AU-rich element (ARE) of tumor necrosis factor alpha (TNFα), a well-known RNA motif that induces mRNA degradation, via 4×S1m to a SA matrix, and used the resulting RNA affinity column to purify ARE-binding proteins (BPs) from cellular extracts. By quantitative mass spectrometry using differential dimethyl labeling, we identified the majority of established ARE-BPs and detected several RNA-BPs that had previously not been associated with AREs. For two of these proteins, Rbms1 and Roxan, we confirmed specific binding to the TNFα ARE. The optimized 4×S1m aptamer, therefore, provides a powerful tool for the discovery of mRNP components in a single affinity purification step." @default.
• W2146372143 created "2016-06-24" @default.
• W2146372143 creator A5013622991 @default.
• W2146372143 creator A5033109401 @default.
• W2146372143 date "2013-10-23" @default.
• W2146372143 modified "2023-10-14" @default.
• W2146372143 title "An optimized streptavidin-binding RNA aptamer for purification of ribonucleoprotein complexes identifies novel ARE-binding proteins" @default.
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• W2146372143 doi "https://doi.org/10.1093/nar/gkt956" @default.
• W2146372143 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3902943" @default.
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• W2146372143 hasPublicationYear "2013" @default.
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