Binding Specificities of Human RNA-Binding Proteins Toward Structured and Linear RNA Sequences
Downloaded from genome.cshlp.org on September 29, 2021 - Published by Cold Spring Harbor Laboratory Press Research Binding specificities of human RNA-binding proteins toward structured and linear RNA sequences Arttu Jolma,1,11 Jilin Zhang,1,11 Estefania Mondragón,2,11 Ekaterina Morgunova,1 Teemu Kivioja,3 Kaitlin U. Laverty,4 Yimeng Yin,1 Fangjie Zhu,1 Gleb Bourenkov,5 Quaid Morris,4,6,7,8,9 Timothy R. Hughes,4,6 Louis James Maher III,2 and Jussi Taipale1,3,10 1Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-171 77, Solna, Sweden; 2Department of Biochemistry and Molecular Biology, Mayo Clinic Graduate School of Biomedical Sciences, Mayo Clinic College of Medicine and Science, Rochester, Minnesota 55905, USA; 3Genome-Scale Biology Program, University of Helsinki, FI-00014, Helsinki, Finland; 4Department of Molecular Genetics, University of Toronto, M5S 1A8, Toronto, Canada; 5European Molecular Biology Laboratory (EMBL), Hamburg Unit c/o DESY, D-22603 Hamburg, Germany; 6Donnelly Centre, University of Toronto, M5S 3E1, Toronto, Canada; 7Edward S. Rogers Sr. Department of Electrical and Computer Engineering, University of Toronto, M5S 3G4, Toronto, Canada; 8Department of Computer Science, University of Toronto, M5S 2E4, Toronto, Canada; 9Memorial Sloan Kettering Cancer Center, New York, New York 10065, USA; 10Department of Biochemistry, University of Cambridge, CB2 1QW, Cambridge, United Kingdom RNA-binding proteins (RBPs) regulate RNA metabolism at multiple levels by affecting splicing of nascent transcripts, RNA folding, base modification, transport, localization, translation, and stability. Despite their central role in RNA function, the RNA-binding specificities of most RBPs remain unknown or incompletely defined. To address this, we have assembled a genome-scale collection of RBPs and their RNA-binding domains (RBDs) and assessed their specificities using high-through- put RNA-SELEX (HTR-SELEX).
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