Intrinsically Disordered Protein Ntr2 Modulates the Spliceosomal RNA Helicase Brr2.

ABSTRACT: Precursor messenger RNA splicing is mediated by the spliceosome, a large and dynamic molecular machine composed of five small nuclear RNAs and numerous proteins. Many spliceosomal proteins are predicted to be intrinsically disordered or contain large disordered regions, but experimental validation of these predictions is scarce, and the precise functions of these proteins are often unclear. Here, we show via circular dichroism spectroscopy, dynamic light scattering, and NMR spectroscopy that the yeast spliceosomal disassembly factor Ntr2 is largely intrinsically disordered. Peptide SPOT analyses, analytical size-exclusion chromatography, and surface plasmon resonance measurements revealed that Ntr2 uses an N-terminal region to bind the C-terminal helicase unit of the Brr2 RNA helicase, an

SUBMITTER: Wollenhaupt J 

PROVIDER: S-EPMC5984983 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature