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A comprehensive review of methods to study lncRNA-protein interactions in solution

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BIOCHEMICAL SOCIETY TRANSACTIONS
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PORTLAND PRESS LTD
DOI: 10.1042/BST20220604

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Recent studies have shown that long non-coding RNAs (lncRNAs) play crucial roles in genomic maintenance and disease progression. Due to their length, lncRNAs have complex folded structures and interactions with various biomolecules, enabling them to carry out diverse biological functions.
The long non-coding RNAs (lncRNAs) other than rRNA and tRNA were earlier assumed to be 'junk genomic material'. However, recent advancements in genomics methods have highlighted their roles not only in housekeeping but also in the progression of diseases like cancer as well as viral infections. lncRNAs owing to their length, have both short-range and long-range interactions resulting in complex folded structures that recruit various biomolecules enabling lncRNAs to undertake their various biological functions. Using cell lysate pull-down assays increasing number of lnRNAs-interacting proteins are being identified. These interactions can be further exploited to develop targeted novel therapeutic strategies to inhibit lncRNA-protein interactions. This review attempts to suc-cinctly techniques that can identify and characterize the lnRNAs-protein interactions (i.e. affinity, stoichiometry, and thermodynamics). Furthermore, using other sophisticated bio-physical techniques, one can also perform size estimations, and determine low-resolution structures. Since these methods study the biomolecules in solution, large-scale structural observations can be performed in real-time. This review attempts to briefly introduce the readers to biochemical and biophysical techniques, such that they can utilize these methods to obtain a holistic characterization of the biomolecules of interest. Additionally, it should be noted that the use of these methods is not limited to the characterization of the interacting molecules but can also be used to determine the efficacy of the thera-peutic molecules to disrupt these interactions.

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