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Nat Methods ; 14(5): 487-490, 2017 May.
Article in English | MEDLINE | ID: mdl-28346450

ABSTRACT

Ribonucleoproteins (RNPs) are key regulators of cellular function. We established an efficient approach, crosslinking of segmentally isotope-labeled RNA and tandem mass spectrometry (CLIR-MS/MS), to localize protein-RNA interactions simultaneously at amino acid and nucleotide resolution. The approach was tested on polypyrimidine tract binding protein 1 and U1 small nuclear RNP. Our method provides distance restraints to support integrative atomic-scale structural modeling and to gain mechanistic insights into RNP-regulated processes.


Subject(s)
Heterogeneous-Nuclear Ribonucleoproteins/chemistry , Models, Molecular , Nucleic Acid Conformation , Polypyrimidine Tract-Binding Protein/chemistry , RNA/chemistry , Ribonucleoprotein, U1 Small Nuclear/chemistry , Binding Sites , Carbon Isotopes , Chromatography, High Pressure Liquid , Heterogeneous-Nuclear Ribonucleoproteins/genetics , Nitrogen Isotopes , Nuclear Magnetic Resonance, Biomolecular , Polypyrimidine Tract-Binding Protein/genetics , Protein Binding , Ribonucleoprotein, U1 Small Nuclear/genetics , Software , Tandem Mass Spectrometry , Ultraviolet Rays
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