ArticleNucleic acids research2019
Increased versatility despite reduced molecular complexity: evolution, structure and function of metazoan splicing factor PRPF39.
Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 18 citations in OpenAlex.
- TRNAU1AP and PRPF39 establish integrated control over processing of most abundant human non-coding RNAs.Nature communications · 2026Article
- Identification and clustering analysis of drug-responsive temporally varying genes through high-frequency longitudinal RNA sequencing.Scientific reports · 2026Article
- Identification of copper death-associated molecular clusters and immunological profiles in rheumatoid arthritis.Frontiers in immunology · 2023Article
- The U1 snRNP component RBP45d regulates temperature-responsive flowering in Arabidopsis.The Plant cell · 2022Article
- A genetic screen in Arabidopsis reveals the identical roles for RBP45d and PRP39a in 5' cryptic splice site selection.Frontiers in plant science · 2022Article
- Alternative splicing level related to intron size and organism complexity.BMC genomics · 2021Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the yeast U1 snRNP the Prp39/Prp42 heterodimer is essential for early steps of spliceosome assembly. In metazoans no Prp42 ortholog exists, raising the question how the heterodimer is functionally substituted. Here we present the crystal structure of murine PRPF39, which forms a homodimer. Structure-guided point mutations disrupt dimer formation and inhibit splicing, manifesting the homodimer as functional unit. PRPF39 expression is controlled by NMD-inducing alternative splicing in mice and human, suggesting a role in adapting splicing efficiency to cell type specific requirements. A phylogenetic analysis reveals coevolution of shortened U1 snRNA and the absence of Prp42, which correlates with overall splicing complexity in different fungi. While current models correlate the diversity of spliceosomal proteins with splicing complexity, our study highlights a contrary case. We find that organisms with higher splicing complexity have substituted the Prp39/Prp42 heterodimer with a PRPF39 homodimer.
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Registered trials
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