Group Leader, Transcription RegulationLa, ICGEB New Delhi, INDIA
Fascinating mechanism of single-stranded nucleic acid recognition by RNA Recognition Motifs
Host: G. Del Sal
RNA binding proteins or RBPs play an indispensable role in cellular machinery, especially processes such as transcription, post-transcriptional modification of RNA, RNA transport, and stabilization. Post-transcriptional modifications of RNA are a major route through which eukaryotes regulate gene expression. These modifications include splicing, mRNA polyadenylation, 5’ capping, and RNA editing. RBPs bind DNA and RNA through specific RNA binding domains (RBDs) or modules. Binding affinities and specificities vary throughout this family of proteins. The RNA recognition motif, or RRM, is the most widely distributed RBD in nature. RRMs are canonically identified through the presence of two RNA binding consensus motifs (RNP). They have a typical three-dimensional architecture, which classically consists of a four-stranded β-sheet supported by two α-helices, with the β-sheet serving as the primary surface for nucleic-acid recognition.
Despite these unifying traits of RRMs, they possess remarkably diverse DNA and RNA recognition capabilities. Our recent structural studies on DNA and RNA recognition by RRMs paint an interesting picture of how a single fold is able to recognize different cognate RNAs and DNAs by virtue of minor but crucial alterations to its binding surface. In addition, delineating nucleic acid binding specificities of RRMs has provided molecular clues to the progression of debilitating diseases.
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