RNA-binding proteins (RBPs) are integral components of cellular machinery, playing crucial roles in the regulation of gene expression and maintaining genetic stability. Their interactions with RNA molecules govern critical processes such as mRNA splicing, stability, localization, and translation, which are essential for proper cellular function. These proteins interact with RNA molecules and other proteins to form ribonucleoprotein complexes (RNPs), hence controlling the fate of target RNAs. The interaction occurs via RNA recognition motif, the zinc finger domain, the KH domain and the double stranded RNA binding motif (all known as RNA-binding domains (RBDs). These domains are found within the coding sequences (intron and exon domains), 5’ untranslated regions (5’UTR) and 3’ untranslated regions (3’UTR). Dysregulation of RBPs can lead to genomic instability, contributing to various pathologies, including cancer neurodegenerative diseases, and metabolic disorders. This study comprehensively explores the multifaceted roles of RBPs in genetic stability, highlighting their involvement in maintaining genomic integrity through modulation of RNA processing and their implications in cellular signalling pathways. Furthermore, it discusses how aberrant RBP function can precipitate genetic instability and disease progression, emphasizing the therapeutic potential of targeting RBPs in restoring cellular homeostasis. Through an analysis of current literature, this study aims to delineate the critical role of RBPs in ensuring genetic stability and their promise as targets for innovative therapeutic strategies.

The emergence of multidrug-resistant Neisseria gonorrhoeae has intensified the need for innovative therapeutic strategies. One promising but underexplored target is the Hfq protein, a key regulator in bacterial stress response and pathogenesis. In this study, we employed a computer-aided drug discovery approach to screen phytochemicals from traditionally used anti-gonorrheal plants for their potential to inhibit Hfq. Molecular docking identified several compounds, including Hellebrigenin 3-acetate, Carpaine, β-amyrin, α-amyrin, Rosarin, Oleanolic acid, and Epigallocatechin 3-O-gallate, with binding affinities surpassing that of the reference drug, Ceftriaxone. Molecular dynamics simulations revealed that Carpaine and Oleanolic acid formed the most stable Hfq complexes, exhibiting low RMSD values (0.73 nm and 0.66 nm) and compact Rg profiles (~ 1.4 nm), indicating strong structural stabilization. ADMET analysis suggested moderate intestinal absorption and oral bioavailability, though some compounds showed risks of liver toxicity and CYP2D6 inhibition. Carpaine demonstrated the most favorable binding free energy and prolonged systemic retention, making it an up-and-coming lead candidate. Importantly, evolutionary analysis confirmed the conservation of the Hfq active site, further supporting its viability as a therapeutic target. These findings reveal the potential of plant-derived compounds, particularly Carpaine and Oleanolic acid, as novel Hfq inhibitors, providing a strong foundation for future experimental validation and the development of alternative therapies against multidrug-resistant N. gonorrhoeae.

Tuberculosis (TB) remains a major public health challenge in sub-Saharan Africa, where it contributes significantly to morbidity and mortality. Traditional