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Systematic analysis of the impact of R-methylation on RBPs-RNA interactions

ABSTRACT: RNA binding proteins (RBPs) bind RNAs through specific RNA-binding domains, generating multi-molecular complexes known as ribonucleoproteins (RNPs). Various post-translational modifications (PTMs) have been described to regulate RBP structure, subcellular localization and interactions with other proteins or RNAs. Recent proteome-wide experiments showed that RBPs are the most representative group within the class of arginine (R)-methylated proteins; moreover, emerging evidence suggests that this modification plays a major role in the regulation of RBP-RNA interaction. Nevertheless, a systematic analysis of how changes in protein-R-methylation can affect globally RBPs-RNA interactions has not yet been carried out. We describe here a quantitative proteomics approach to profile global changes of RBP-RNA interactions upon the modulation of protein arginine methyltransferases PRMT1 and PRMT5. By coupling the recently described Orthogonal Organic Phase Separation (OOPS) with SILAC labelling and pharmacological modulation of PRMT1 and PRMT5 enzyme, we describe the RNA-binding protein dynamics in dependence of protein-R-methylation.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture, Hela Cell

SUBMITTER: Enrico Massignani

LAB HEAD: Tiziana Bonaldi

PROVIDER: PXD024601 | Pride | 2021-08-25

REPOSITORIES: Pride

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			Action	DRS
	HF201110_MM33_A1.raw	Raw
	HF201110_MM33_A2.raw	Raw
	HF201110_MM33_A3.raw	Raw
	HF201110_MM33_A4.raw	Raw
	HF201110_MM33_A5.raw	Raw

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