Ask about this productRelated genes to: RBM41 antibody
- Gene:
- RBM41 NIH gene
- Name:
- RNA binding motif protein 41
- Previous symbol:
- -
- Synonyms:
- FLJ11016
- Chromosome:
- Xq22.3
- Locus Type:
- gene with protein product
- Date approved:
- 2006-07-11
- Date modifiied:
- 2014-11-18
Related products to: RBM41 antibody
Related articles to: RBM41 antibody
- Pre-mRNA introns are removed by two distinct spliceosomes: the major (U2-type) spliceosome, which splices over 99.5% of introns, and the minor (U12-type) spliceosome, responsible for a rare class of introns known as minor introns. While the major spliceosome contains U1, U2, U4, U5, and U6 small nuclear RNAs (snRNAs) along with numerous associated proteins, the minor spliceosome comprises U11, U12, U4atac, U5, and U6atac snRNAs and includes specialized proteins. The function and regulation of the minor spliceosome are critical. Mutations in its specific component, RNA-binding protein RNPC3/65K, are linked to human diseases such as primary ovarian insufficiency. In this study, we identify RNA-binding protein Miso (CG44249), which shares 31% and 27% amino acid sequence identity with human RNPC3 and RBM41, respectively, as a key factor in minor splicing and oogenesis in Miso associates with U11 and U12 snRNAs in ovaries. mutant females exhibit smaller ovaries, reduced germline stem cell numbers, disrupted oogenesis, reduced fecundity, and lower fertility. In mutant ovaries, significant minor intron retention is observed, accompanied by a reduction in spliced RNAs and protein products. Our findings establish Miso as a critical factor for minor intron splicing and underscore its essential role in oogenesis. - Source: PubMed
Publication date: 2025/05/16
Taira YukiZhu LiFukunaga Ryuya - Here, we identify RBM41 as a novel unique protein component of the minor spliceosome. RBM41 has no previously recognized cellular function but has been identified as a paralog of U11/U12-65K, a known unique component of the U11/U12 di-snRNP. Both proteins use their highly similar C-terminal RRMs to bind to 3'-terminal stem-loops in U12 and U6atac snRNAs with comparable affinity. Our BioID data indicate that the unique N-terminal domain of RBM41 is necessary for its association with complexes containing DHX8, an RNA helicase, which in the major spliceosome drives the release of mature mRNA from the spliceosome. Consistently, we show that RBM41 associates with excised U12-type intron lariats, is present in the U12 mono-snRNP, and is enriched in Cajal bodies, together suggesting that RBM41 functions in the post-splicing steps of the minor spliceosome assembly/disassembly cycle. This contrasts with U11/U12-65K, which uses its N-terminal region to interact with U11 snRNP during intron recognition. Finally, while RBM41 knockout cells are viable, they show alterations in U12-type 3' splice site usage. Together, our results highlight the role of the 3'-terminal stem-loop of U12 snRNA as a dynamic binding platform for the U11/U12-65K and RBM41 proteins, which function at distinct stages of the assembly/disassembly cycle. - Source: PubMed
Norppa Antto JChowdhury Iftekharvan Rooijen Laura ERavantti Janne JSnel BerendVarjosalo MarkkuFrilander Mikko J