Castello, A;
Fischer, B;
Frese, CK;
Horos, R;
Alleaume, A-M;
Foehr, S;
Curk, T;
... Hentze, MW; + view all
(2016)
Comprehensive Identification of RNA-Binding Domains in Human Cells.
Molecular Cell
, 63
(4)
pp. 696-710.
10.1016/j.molcel.2016.06.029.
Preview |
Text
Castello_1-s2.0-S1097276516302878-main.pdf - Published Version Download (6MB) | Preview |
Abstract
Mammalian cells harbor more than a thousand RNA-binding proteins (RBPs), with half of these employing unknown modes of RNA binding. We developed RBDmap to determine the RNA-binding sites of native RBPs on a proteome-wide scale. We identified 1,174 binding sites within 529 HeLa cell RBPs, discovering numerous RNA-binding domains (RBDs). Catalytic centers or protein-protein interaction domains are in close relationship with RNA-binding sites, invoking possible effector roles of RNA in the control of protein function. Nearly half of the RNA-binding sites map to intrinsically disordered regions, uncovering unstructured domains as prevalent partners in protein-RNA interactions. RNA-binding sites represent hot spots for defined posttranslational modifications such as lysine acetylation and tyrosine phosphorylation, suggesting metabolic and signal-dependent regulation of RBP function. RBDs display a high degree of evolutionary conservation and incidence of Mendelian mutations, suggestive of important functional roles. RBDmap thus yields profound insights into native protein-RNA interactions in living cells.
| Type: | Article |
|---|---|
| Title: | Comprehensive Identification of RNA-Binding Domains in Human Cells |
| Location: | United States |
| Open access status: | An open access version is available from UCL Discovery |
| DOI: | 10.1016/j.molcel.2016.06.029 |
| Publisher version: | http://doi.org/10.1016/j.molcel.2016.06.029 |
| Language: | English |
| Additional information: | Copyright © 2016 The Author(s). Published by Elsevier Inc. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
| Keywords: | Acetylation, Computational Biology, Databases, Protein, Evolution, Molecular, HeLa Cells, Humans, Methylation, Models, Molecular, Mutation, Nucleic Acid Conformation, Phosphorylation, Protein Binding, Protein Interaction Domains and Motifs, Protein Processing, Post-Translational, Proteomics, RNA, RNA-Binding Motifs, RNA-Binding Proteins, Structure-Activity Relationship |
| URI: | https://discovery.ucl.ac.uk/id/eprint/10064010 |
Archive Staff Only
 |
View Item |
