PRP8 Antibody

1. error-prone/efficient RH alleles suppress a prp2 mutant deficient at promoting the first catalytic step of splicing, whereas hyperaccurate/inefficient RH alleles exhibit synthetic sickness. Together our data indicate that prp8 RH alleles link splicing fidelity with catalytic efficiency by biasing the relative stabilities of distinct spliceosome conformations. PMID: 28416677
2. Together, these data establish that PRP8 is a metalloprotein that promotes exon ligation within the spliceosome. PMID: 23686287
3. Prp8 interaction sites with Snu114 and Aar2 proteins PMID: 16373487
4. Our results define a new ubiquitin-binding domain of Prp8 and suggest functional links between ubiquitin and the pre-mRNA splicing machinery PMID: 16428608
5. The expanded Prp8 Jab1/MPN domain represents a pseudoenzyme converted into a protein-protein interaction platform and that dysfunction of this platform underlies Retinitis pigmentosa. PMID: 17317632
6. Opposing classes of prp8 alleles modulate the transition between the catalytic steps of pre-mRNA splicing. PMID: 17486100
7. evidence for a cytoplasmic precursor U5 snRNP that lacks mature U5 snRNP component Brr2p & depends on nuclear localization signal in Prp8p for nuclear import; retinitis pigmentosa mutations in Prp8p result in nuclear accumulation of precursor U5 snRNP PMID: 17934474
8. possible mechanism of how Prp8 regulates spliceosome activation PMID: 18779563
9. Results suggest that domain IV of PRP8 forms a surface that interacts directly with the RNA structures at the catalytic core of the spliceosome. PMID: 18836455
10. Crystal structures of corresponding portions of yeast and human Prp8 that interact with functional regions of the pre-mRNA were determined, revealing a phylogenetically conserved RNase H fold, augmented by Prp8-specific elements. PMID: 18843295

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KEGG: sce:YHR165C

STRING: 4932.YHR165C