期刊
MOLECULAR CELL
卷 63, 期 4, 页码 696-710出版社
CELL PRESS
DOI: 10.1016/j.molcel.2016.06.029
关键词
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资金
- MRC Career Development Award [MR/L019434/1]
- ERC Advanced Grant [ERC-2011-ADG_20110310]
- Virtual Liver Network of the German Ministry for Science and Education
- EMBO postdoctoral fellowship [LTF1006-2013]
- Medical Research Council [MR/L019434/1] Funding Source: researchfish
- MRC [MR/L019434/1, MC_UU_12014/10] Funding Source: UKRI
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.
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