RNA recognition by Npl3p reveals U2 snRNA-binding compatible with a chaperone role during splicing.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
07 11 2023
07 11 2023
Historique:
received:
31
08
2022
accepted:
27
10
2023
medline:
9
11
2023
pubmed:
8
11
2023
entrez:
7
11
2023
Statut:
epublish
Résumé
The conserved SR-like protein Npl3 promotes splicing of diverse pre-mRNAs. However, the RNA sequence(s) recognized by the RNA Recognition Motifs (RRM1 & RRM2) of Npl3 during the splicing reaction remain elusive. Here, we developed a split-iCRAC approach in yeast to uncover the consensus sequence bound to each RRM. High-resolution NMR structures show that RRM2 recognizes a 5´-GNGG-3´ motif leading to an unusual mille-feuille topology. These structures also reveal how RRM1 preferentially interacts with a CC-dinucleotide upstream of this motif, and how the inter-RRM linker and the region C-terminal to RRM2 contribute to cooperative RNA-binding. Structure-guided functional studies show that Npl3 genetically interacts with U2 snRNP specific factors and we provide evidence that Npl3 melts U2 snRNA stem-loop I, a prerequisite for U2/U6 duplex formation within the catalytic center of the B
Identifiants
pubmed: 37935663
doi: 10.1038/s41467-023-42962-4
pii: 10.1038/s41467-023-42962-4
pmc: PMC10630445
doi:
Substances chimiques
Ribonucleoprotein, U2 Small Nuclear
0
RNA
63231-63-0
RNA, Small Nuclear
0
U2 small nuclear RNA
0
NPL3 protein, S cerevisiae
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
7166Informations de copyright
© 2023. The Author(s).
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