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- W3146294505 abstract "Protein binding is essential to the transport, decay and regulation of almost all RNA molecules. However, the structural pref- erence of protein binding on RNAs and their cellular functions and dynamics upon changing environmental conditions are poorly understood. Here, we integrated various high-throughput data and introduced a computational framework to describe the global interactions between RNA binding proteins(RBPs) and structured RNAs in yeast at single-nucleotide resolution. We found that on average, in terms of percent total lengths, ~15% of mRNA untranslated regions(UTRs), ~37% of canonical non-coding RNAs(ncRNAs) and ~11% of long ncRNAs(lncRNAs) are bound by proteins. The RBP binding sites, in general, tend to occur at single-stranded loops, with evolutionarily conserved signatures, and often facilitate a specific RNA structure conformation in vivo. We found that four nucleotide modifications of tRNA are significantly associated with RBP binding. We also identified various structural motifs bound by RBPs in the UTRs of mRNAs, associated with localization, degradation and stress responses. Moreover, we identified 200 novel lncRNAs bound by RBPs, and about half of them contain conserved secondary structures. We present the first ensemble pattern of RBP binding sites in the structured non-coding regions of a eu- karyotic genome, emphasizing their structural context and cellular functions." @default.
- W3146294505 created "2021-04-13" @default.
- W3146294505 creator A5069039059 @default.
- W3146294505 date "2014-01-01" @default.
- W3146294505 modified "2023-09-24" @default.
- W3146294505 title "Global signatures of protein binding on structured RNAs in Saccharomyces cerevisiae" @default.
- W3146294505 hasPublicationYear "2014" @default.
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