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Deciphering the protein-RNA recognition code: Combining large-scale quantitative methods with structural biology.

Bioessays 37, 899-908 (2015)
DOI
Open Access Green as soon as Postprint is submitted to ZB.
RNA binding proteins (RBPs) are key factors for the regulation of gene expression by binding to cis elements, i.e. short sequence motifs in RNAs. Recent studies demonstrate that cooperative binding of multiple RBPs is important for the sequence-specific recognition of RNA and thereby enables the regulation of diverse biological activities by a limited set of RBPs. Cross-linking immuno-precipitation (CLIP) and other recently developed high-throughput methods provide comprehensive, genome-wide maps of protein-RNA interactions in the cell. Structural biology gives detailed insights into molecular mechanisms and principles of RNA recognition by RBPs, but has so far focused on single RNA binding proteins and often on single RNA binding domains. The combination of high-throughput methods and detailed structural biology studies is expected to greatly advance our understanding of the code for protein-RNA recognition in gene regulation, as we review in this article.
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Publication type Article: Journal article
Document type Scientific Article
Corresponding Author
Keywords Clip ; Cooperativity ; Mrna Interactome ; Protein-rna Recognition ; Rna Binding Proteins ; Rna Recognition Motif ; Structural Biology; Transcriptome-wide Identification; Single-nucleotide Resolution; Splicing Factor U2af65; Embryonic Stem-cells; Factor-binding Sites; Msl-2 Messenger-rna; Cold-shock Protein; Crystal-structure; Sex-lethal; Molecular-basis
ISSN (print) / ISBN 0265-9247
e-ISSN 1521-1878
Journal BioEssays
Quellenangaben Volume: 37, Issue: 8, Pages: 899-908 Article Number: , Supplement: ,
Publisher Wiley
Publishing Place Hoboken
Non-patent literature Publications
Reviewing status Peer reviewed