Intrinsically Disordered Protein Ntr2 Modulates the Spliceosomal RNA Helicase Brr2.

摘要: Abstract Precursor messenger RNA splicing is mediated by the spliceosome, a large and dynamic molecular machine composed of five small nuclear RNAs numerous proteins. Many spliceosomal proteins are predicted to be intrinsically disordered or contain regions, but experimental validation these predictions scarce, precise functions often unclear. Here, we show via circular dichroism spectroscopy, light scattering, NMR spectroscopy that yeast disassembly factor Ntr2 largely disordered. Peptide SPOT analyses, analytical size-exclusion chromatography, surface plasmon resonance measurements revealed uses an N-terminal region bind C-terminal helicase unit Brr2 helicase, enzyme involved in spliceosome activation implicated catalysis disassembly. analyses suggested does not adopt tertiary structure likely remains upon complex formation. binding unwinding studies showed downregulates activity in vitro modulating fraction molecules productively bound substrate. Our data clarify nature physical link between Ntr2, point possibility functional Ntr2-Brr2 interplay during splicing.