Journal
RNA
Volume 23, Issue 6, Pages 968-981Publisher
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1261/rna.059378.116
Keywords
splicing; U2 snRNP; SF3b; RNA binding; RRM
Categories
Funding
- Medical Research Council [MC_U105184330]
- Wellcome Trust
- MRC career development fellowship
- Humanitas Research Foundation
- CNRS
- CERBM-IGBMC
- INSERM
- French State fund
- Ligue Contre le Cancer
- [ANR-10LABX-0030-INRT]
- [ANR-10-IDEX-0002-02]
- MRC [MC_U105184330] Funding Source: UKRI
- Medical Research Council [MC_U105184330] Funding Source: researchfish
Ask authors/readers for more resources
Spliceosomal proteins Hsh49p and Cus1p are components of SF3b, which together with SF3a, Msl1p/Lea1p, Sm proteins, and U2 snRNA, form U2 snRNP, which plays a crucial role in pre-mRNA splicing. Hsh49p, comprising two RRMs, forms a heterodimer with Cus1p. We determined the crystal structures of Saccharomyces cerevisiae full-length Hsh49p as well as its RRM1 in complex with a minimal binding region of Cus1p (residues 290-368). The structures show that the Cus1 fragment binds to the a-helical surface of Hsh49p RRM1, opposite the four-stranded beta-sheet, leaving the canonical RNA-binding surface available to bind RNA. Hsh49p binds the 5' end region of U2 snRNA via RRM1. Its affinity is increased in complex with Cus1(290-368)p, partly because an extended RNA-binding surface forms across the protein-protein interface. The Hsh49p RRM1-Cus1(290-368)p structure fits well into cryo-EM density of the B-act spliceosome, corroborating the biological relevance of our crystal structure.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available