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Distinct functions for the paralogous RBM41 and U11/U12-65K proteins in the minor spliceosome
Antto J Norppa1, Iftekhar Chowdhury2, Laura E van Rooijen3
1Institute of Biotechnology, University of Helsinki, Helsinki, Finland.
Nucleic Acids Research
|March 18, 2024
Summary
Researchers identified RBM41 as a new protein in the minor spliceosome. This protein binds to U12 and U6atac snRNAs, suggesting a role in post-splicing events and alternative splicing regulation.
Area of Science:
- Molecular Biology
- RNA Biology
- Gene Regulation
Background:
- The minor spliceosome is crucial for processing specific introns.
- Unique protein components of the minor spliceosome are not fully understood.
- RBM41 is a paralog of U11/U12-65K, a known minor spliceosome component.
Purpose of the Study:
- To identify novel protein components of the minor spliceosome.
- To elucidate the function of RBM41 within the minor spliceosome.
- To investigate the role of RBM41 in splicing regulation.
Main Methods:
- BioID proximity labeling to identify interacting proteins.
- RNA-binding assays to assess snRNA interaction.
- Immunofluorescence to determine subcellular localization.
- Analysis of RBM41 knockout cells for splicing defects.
Main Results:
- RBM41 is a novel component of the minor spliceosome, binding U12 and U6atac snRNAs via its RRM domain.
- RBM41's N-terminal domain mediates interaction with DHX8 and associates with intron lariats.
- RBM41 knockout cells exhibit altered U12-type 3' splice site usage.
Conclusions:
- RBM41 functions in the post-splicing stages of the minor spliceosome cycle.
- The 3'-terminal stem-loop of U12 snRNA serves as a dynamic platform for RBM41 and U11/U12-65K.
- RBM41 plays a role in regulating alternative splicing of U12-dependent introns.
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