ArticleProceedings of the National Academy of Sciences of the United States of America2004
Effects of the U1C L13 mutation and temperature regulation of yeast commitment complex formation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 21 citations in OpenAlex.
- Article
- Article
- Oncogenic fusion protein EWS-FLI1 is a network hub that regulates alternative splicing.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The spliceosome: disorder and dynamics defined.Current opinion in structural biology · 2014Review
- Differentially expressed, variant U1 snRNAs regulate gene expression in human cells.Genome research · 2013Article
- DExD/H-box Prp5 protein is in the spliceosome during most of the splicing cycle.RNA (New York, N.Y.) · 2009Article
- A targeted bypass screen identifies Ynl187p, Prp42p, Snu71p, and Cbp80p for stable U1 snRNP/Pre-mRNA interaction.Molecular and cellular biology · 2009Article
- The U11-48K protein contacts the 5' splice site of U12-type introns and the U11-59K protein.Molecular and cellular biology · 2008Article
- The U1, U2 and U5 snRNAs crosslink to the 5' exon during yeast pre-mRNA splicing.Nucleic acids research · 2008Article
- Remodeling of ribonucleoprotein complexes with DExH/D RNA helicases.Nucleic acids research · 2006Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The U1 small nuclear ribonucleoprotein particle U1C protein has a zinc finger-like structure (C2H2 motif) at its N terminus, which is conserved from yeast to humans. Mutations of amino acid L13 within this domain rescue the essential function of the helicase protein Prp28p. Prp28p has been implicated in unwinding the 5' splice site (5'ss)-U1 small nuclear RNA (snRNA) base-pairing, to allow replacement of U1 snRNA with U6 snRNA during spliceosome assembly. The L13 phenotype has therefore been interpreted to indicate that WT U1C contributes to 5'ss-U1 snRNA stabilization by binding to the RNA duplex. We show here that an L13 mutant extract cannot form stable base-pairing at room temperature but is permissive for U1-5'ss base-pairing at low temperature. This phenotype is similar to that of a U1C-depleted extract, indicating that the U1C L13 mutation is a strong loss-of-function mutation. The two mutant extracts are unlike a WT extract, which undergoes stable pairing at room temperature but little or no pairing at low temperature. Taken together with previous results and the failure to observe a direct interaction of U1C with the U1-5'ss duplex, the data suggest that U1C contributes indirectly to stable U1-5'ss base-pairing under permissive conditions. A model is proposed to account for the L13 results.
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