ArticleProceedings of the National Academy of Sciences of the United States of America2000
Crystal structure of the functional domain of the splicing factor Prp18.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 25 citations in OpenAlex.
- Splicing factor Prp18p promotes genome-wide fidelity of consensus 3'-splice sites.Nucleic acids research · 2023Article
- Postcatalytic spliceosome structure reveals mechanism of 3'-splice site selection.Science (New York, N.Y.) · 2017Article
- Article
- The Fission Yeast Pre-mRNA-processing Factor 18 (prp18+) Has Intron-specific Splicing Functions with Links to G1-S Cell Cycle Progression.The Journal of biological chemistry · 2016Article
- Functional interactions between Prp8, Prp18, Slu7, and U5 snRNA during the second step of pre-mRNA splicing.RNA (New York, N.Y.) · 2007Article
- The Prp18 protein stabilizes the interaction of both exons with the U5 snRNA during the second step of pre-mRNA splicing.Genes & development · 2007Article
- Genetic and functional interaction of evolutionarily conserved regions of the Prp18 protein and the U5 snRNA.Molecular and cellular biology · 2005Article
- Splicing factor hSlu7 contains a unique functional domain required to retain the protein within the nucleus.Molecular biology of the cell · 2004Article
- Mutational analysis identifies two separable roles of the Saccharomyces cerevisiae splicing factor Prp18.RNA (New York, N.Y.) · 2002Article
- A cyclophilin functions in pre-mRNA splicing.The EMBO journal · 2002Article
- Genome-wide gene expression profiles of the developing mouse hippocampus.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The splicing factor Prp18 is required for the second step of pre-mRNA splicing. We have isolated and determined the crystal structure of a large fragment of the Saccharomyces cerevisiae Prp18 that lacks the N-terminal 79 amino acids. This fragment, called Prp18Delta79, is fully active in yeast splicing in vitro and includes the sequences of Prp18 that have been evolutionarily conserved. The core structure of Prp18Delta79 is compact and globular, consisting of five alpha-helices that adopt a novel fold that we have designated the five-helix X-bundle. The structure suggests that one face of Prp18 interacts with the splicing factor Slu7, whereas the more evolutionarily conserved amino acids in Prp18 form the opposite face. The most highly conserved region of Prp18, a nearly invariant stretch of 19 aa, forms part of a loop between two alpha-helices and may interact with the U5 small nuclear ribonucleoprotein particles. The structure is consistent with a model in which Prp18 forms a bridge between Slu7 and the U5 small nuclear ribonucleoprotein particles.
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