Stability-Based Proteomics for Investigation of Structured RNA-Protein Interactions.

ABSTRACT: RNA-protein interactions are essential to RNA function throughout biology. Identifying the protein interactions associated with a specific RNA, however, is currently hindered by the need for RNA labeling or costly tiling-based approaches. Conventional strategies, which commonly rely on affinity pull-down approaches, are also skewed to the detection of high affinity interactions and frequently miss weaker interactions that may be biologically important. Reported here is the first adaptation of stability-based mass spectrometry methods for the global analysis of RNA-protein interactions. The stability of proteins from rates of oxidation (SPROX) and thermal protein profiling (TPP) methods are used to identify the protein targets of three RNA ligands, the MALAT1 triple helix (TH), a vir

SUBMITTER: Bailey MA 

PROVIDER: S-EPMC11316846 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature