Rna Binding Proteins
Rna Binding Proteins - Related Videos
12:24
PAR-CliP - A Method to Identify Transcriptome-wide the Binding Sites of RNA Binding Proteins
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Cited by 267 •
2010
RNA transcripts are subject to extensive posttranscriptional regulation that is mediated by a multitude of trans-acting RNA-binding proteins (RBPs). Here we present a generalizable method to identify precisely and on a transcriptome-wide scale the RNA binding sites of RBPs.
05:07
RNA-Protein Pull-Down Assay to Isolate RNA-Binding Proteins via Affinity Extraction
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2025
This video demonstrates an in vitro RNA pull-down assay to identify RNA-binding proteins (RBPs), which interact with the adenylate-uridylate-rich element (ARE) sequences in mRNA. The target RBPs from a cell lysate are mixed with an RNA probe to form RNA-protein complexes. The complexes are isolated via affinity purification utilizing the affinity of the desthiobiotin label of the RNA probe to a streptavidin-labeled magnetic bead.
11:19
Novel RNA-Binding Proteins Isolation by the RaPID Methodology
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2016
RNA-protein interactions lie at the heart of many cellular processes. Here, we describe an in vivo method to isolate specific RNA and identify novel proteins that are associated with it. This could shed new light on how RNAs are regulated in the cell.
10:34
Detection of RNA-binding Proteins by In Vitro RNA Pull-down in Adipocyte Culture
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Cited by 19 •
2016
An RNA pull-down protocol is optimized here for detection of interactions between RNA-binding proteins (RBPs) and noncoding as well as coding RNAs. An RNA fragment from androgen receptor (AR) was used as an example to demonstrate how to retrieve its RBP from lystate of primary brown adipocytes.
06:30
SELEX-Based In Vitro Binding Assay to Identify RNA-Protein Interactions
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2025
In this video, we describe the systematic evolution of ligands by the exponential enrichment (SELEX) method to identify specific RNA-binding sequences for a target protein of interest. The protein is incubated with a large pool of randomized RNA sequences, and the protein-binding RNA sequences are isolated, PCR-amplified, and sequenced to identify their protein-binding sites.
FAQs
Recognition depends on protein domains that interact with specific RNA sequences or structural features. RNA recognition motifs are one example of these domains, allowing a protein to distinguish particular RNA targets rather than binding all RNA indiscriminately. This selectivity helps direct downstream regulation, including changes in splicing, modification, localization, stability, or translation.
A single RNA-binding protein can influence different aspects of an RNA’s life cycle, from processing and modification to movement, degradation, and translation. By altering these steps, the protein helps determine which RNA molecules persist, where they are positioned, and how effectively they are used. This provides coordinated control beyond the initial production of RNA.
RNA-binding proteins may recognize structural features as well as nucleotide sequences. Consequently, changes in how an RNA folds can affect whether a protein can bind and regulate it. Such recognition links RNA shape to outcomes such as altered processing, localization, stability, or translation, making structural features important determinants of post-transcriptional gene regulation.
Regulation of RNA stability influences how long a transcript remains available, whereas regulation of translation affects how efficiently its information is used to produce protein. Together with control of RNA processing and localization, these activities help cells adjust gene expression without necessarily changing the underlying genetic sequence. The resulting changes support development, stress responses, and cellular identity.
Researchers examine how these proteins coordinate RNA processing, movement, stability, and use in different biological settings. Comparing their regulatory roles during development or in cells with distinct identities can reveal how RNA-based control contributes to specialized cellular states. This approach connects individual protein-RNA interactions with broader changes in gene expression and cell behavior.
Abnormal RNA-binding protein activity or disrupted protein-RNA interactions can interfere with the normal regulation of RNA. Because these proteins influence splicing, modification, localization, degradation, and translation, defects may affect multiple stages of gene expression. Studying those disruptions can clarify disease mechanisms and identify how abnormal RNA processing contributes to biological dysfunction.