ArticleRNA (New York, N.Y.)1999
Functional analysis of SNF, the Drosophila U1A/U2B" homolog: identification of dispensable and indispensable motifs for both snRNP assembly and function in vivo.
Article in RNA (New York, N.Y.), 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 25 citations in OpenAlex.
- Phylogenetic analysis and stress response of the plant U2 small nuclear ribonucleoprotein B″ gene family.BMC genomics · 2022Article
- Molecular principles underlying dual RNA specificity in the Drosophila SNF protein.Nature communications · 2018Article
- FgPrp4 Kinase Is Important for Spliceosome B-Complex Activation and Splicing Efficiency in Fusarium graminearum.PLoS genetics · 2016Article
- spenito is required for sex determination in Drosophila melanogaster.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Resurrection of an Urbilaterian U1A/U2B″/SNF protein.Journal of molecular biology · 2013Article
- Sex-lethal enables germline stem cell differentiation by down-regulating Nanos protein levels during Drosophila oogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Human U2B″ protein binding to snRNA stemloops.Biophysical chemistry · 2011Article
- Distinct regulatory programs establish widespread sex-specific alternative splicing in Drosophila melanogaster.RNA (New York, N.Y.) · 2011Article
- PPS, a large multidomain protein, functions with sex-lethal to regulate alternative splicing in Drosophila.PLoS genetics · 2010Article
- Evolution of an RNP assembly system: a minimal SMN complex facilitates formation of UsnRNPs in Drosophila melanogaster.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Functioning of the Drosophila Wilms'-tumor-1-associated protein homolog, Fl(2)d, in Sex-lethal-dependent alternative splicing.Genetics · 2008Article
- Functional redundancy of worm spliceosomal proteins U1A and U2B''.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- The master switch gene sex-lethal promotes female development by negatively regulating the N-signaling pathway.Developmental cell · 2007Article
- Drosophila SPF45: a bifunctional protein with roles in both splicing and DNA repair.PLoS genetics · 2006Article
- The Drosophila U1-70K protein is required for viability, but its arginine-rich domain is dispensable.Genetics · 2004Article
- The Drosophila U2 snRNP protein U2A' has an essential function that is SNF/U2B" independent.Nucleic acids research · 2001Article
- Pre-messenger RNA processing factors in the Drosophila genome.The Journal of cell biology · 2000Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Drosophila, the spliceosomal protein SNF fulfills the functions of two vertebrate proteins, U1 snRNP-UlA and U2 snRNP-U2B". The structure and sequence of SNF, U1A, and U2B" are nearly identical with two RNA recognition motifs (RRM) separated by a short linker region, yet they have different RNA-binding properties: U1A binds U1 snRNA, U2B" binds U2 snRNA, and SNF binds both snRNAs. Structure/function studies on the human proteins have identified motifs in the N-terminal RRM that are critical for RNA-binding specificity but have failed to identify a function for the C-terminal RRM. Interestingly, SNF is chimeric in these motifs, suggesting a basis for its dual specificity. Here, we test the importance of these motifs by introducing site-directed mutations in the snf coding region and examining the effects of these mutations on assembly into the snRNP and on snf function in vivo. We found that an N-terminal RRM mutant protein predicted to eliminate RNA binding still assembles into snRNPs and is capable of rescuing snf's lethal phenotype only if the normally dispensable C-terminal RRM is present. We also found that the mixed motif in the "RNA-specificity" domain is necessary for SNF's dual function whereas the mixed motif in the U2A'-protein-binding region is not. Finally, we demonstrate that animals carrying a snf mutation that converts SNF from a bifunctional protein to a U1 snRNP-specific protein are viable. This unexpected result suggests that SNF's presence within the U2 snRNP is not essential for splicing.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.