Comprehensive identification of RNA-binding domains in human cells

Mammalian cells harbor more than a thousand RNAbinding 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...

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Main Authors: Castello Palomares, A, Fischer, B, Frese, C, Horos, R, Alleaume, A, Foehr, S, Curk, T, Krijgsveld, J, Hentze, M
Format: Journal article
Published: Cell Press 2016
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author Castello Palomares, A
Fischer, B
Frese, C
Horos, R
Alleaume, A
Foehr, S
Curk, T
Krijgsveld, J
Hentze, M
author_facet Castello Palomares, A
Fischer, B
Frese, C
Horos, R
Alleaume, A
Foehr, S
Curk, T
Krijgsveld, J
Hentze, M
author_sort Castello Palomares, A
collection OXFORD
description Mammalian cells harbor more than a thousand RNAbinding 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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spelling oxford-uuid:6f25d6fc-de12-41e9-acaa-88bc17f96c4f2022-03-26T19:28:50ZComprehensive identification of RNA-binding domains in human cellsJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:6f25d6fc-de12-41e9-acaa-88bc17f96c4fSymplectic Elements at OxfordCell Press2016Castello Palomares, AFischer, BFrese, CHoros, RAlleaume, AFoehr, SCurk, TKrijgsveld, JHentze, MMammalian cells harbor more than a thousand RNAbinding 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.
spellingShingle Castello Palomares, A
Fischer, B
Frese, C
Horos, R
Alleaume, A
Foehr, S
Curk, T
Krijgsveld, J
Hentze, M
Comprehensive identification of RNA-binding domains in human cells
title Comprehensive identification of RNA-binding domains in human cells
title_full Comprehensive identification of RNA-binding domains in human cells
title_fullStr Comprehensive identification of RNA-binding domains in human cells
title_full_unstemmed Comprehensive identification of RNA-binding domains in human cells
title_short Comprehensive identification of RNA-binding domains in human cells
title_sort comprehensive identification of rna binding domains in human cells
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