Allosteric regulation of U1 snRNP by splicing regulatory proteins controls spliceosomal assembly.

ABSTRACT: Alternative splicing is responsible for much of the transcriptomic and proteomic diversity observed in eukaryotes and involves combinatorial regulation by many cis-acting elements and trans-acting factors. SR and hnRNP splicing regulatory proteins often have opposing effects on splicing efficiency depending on where they bind the pre-mRNA relative to the splice site. Position-dependent splicing repression occurs at spliceosomal E-complex, suggesting that U1 snRNP binds but cannot facilitate higher order spliceosomal assembly. To test the hypothesis that the structure of U1 snRNA changes during activation or repression, we developed a method to structure-probe native U1 snRNP in enriched conformations that mimic activated or repressed spliceosomal E-complexes. While the core o

SUBMITTER: Shenasa H 

PROVIDER: S-EPMC7491332 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature