Mapping the binding site of snurportin 1 on native U1 snRNP by cross-linking and mass spectrometry.

ABSTRACT: Mass spectrometry allows the elucidation of molecular details of the interaction domains of the individual components in macromolecular complexes subsequent to cross-linking of the individual components. Here, we applied chemical and UV cross-linking combined with tandem mass-spectrometric analysis to identify contact sites of the nuclear import adaptor snurportin 1 to the small ribonucleoprotein particle U1 snRNP in addition to the known interaction of m(3)G cap and snurportin 1. We were able to define previously unknown sites of protein-protein and protein-RNA interactions on the molecular level within U1 snRNP. We show that snurportin 1 interacts with its central m(3)G-cap-binding domain with Sm proteins and with its extreme C-terminus with stem-loop III of U1 snRNA. The crosslinking da

SUBMITTER: Kuhn-Holsken E 

PROVIDER: S-EPMC2938196 | biostudies-literature | 2010 Sep

REPOSITORIES: biostudies-literature