ArticleBMC biochemistry2008
The FF domains of yeast U1 snRNP protein Prp40 mediate interactions with Luc7 and Snu71.
Article in BMC biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 40 citations in OpenAlex.
- Conserved role for spliceosomal component PRPF40A in microexon splicing.RNA (New York, N.Y.) · 2024Article
- RBM25 is required to restrain inflammation via ACLY RNA splicing-dependent metabolism rewiring.Cellular & molecular immunology · 2024Article
- Conserved role for spliceosomal component PRPF40A in microexon splicing.bioRxiv : the preprint server for biology · 2024Article
- Selected humanization of yeast U1 snRNP leads to global suppression of pre-mRNA splicing and mitochondrial dysfunction in the budding yeast.RNA (New York, N.Y.) · 2024Article
- Binding by calmodulin is coupled to transient unfolding of the third FF domain of Prp40A.Protein science : a publication of the Protein Society · 2023Article
- Chromatin-associated microprocessor assembly is regulated by the U1 snRNP auxiliary protein PRP40.The Plant cell · 2022Article
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- Functional analyses of human LUC7-like proteins involved in splicing regulation and myeloid neoplasms.Cell reports · 2021Article
- Differential Transcription and Alternative Splicing in Cotton Underly Specialized Defense Responses Against Pests.Frontiers in plant science · 2020Article
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- Article
- CryoEM structure of Saccharomyces cerevisiae U1 snRNP offers insight into alternative splicing.Nature communications · 2017Article
- Structure-function analysis and genetic interactions of the Luc7 subunit of the Saccharomyces cerevisiae U1 snRNP.RNA (New York, N.Y.) · 2016Article
- Rapid isolation and single-molecule analysis of ribonucleoproteins from cell lysate by SNAP-SiMPull.RNA (New York, N.Y.) · 2015Article
- Mapping the Protein-Protein Interactome Networks Using Yeast Two-Hybrid Screens.Advances in experimental medicine and biology · 2015Review
- Structure-function analysis of the Yhc1 subunit of yeast U1 snRNP and genetic interactions of Yhc1 with Mud2, Nam8, Mud1, Tgs1, U1 snRNA, SmD3 and Prp28.Nucleic acids research · 2014Article
- The LIM domain protein nTRIP6 recruits the mediator complex to AP-1-regulated promoters.PloS one · 2014Article
- Specific interaction of the transcription elongation regulator TCERG1 with RNA polymerase II requires simultaneous phosphorylation at Ser2, Ser5, and Ser7 within the carboxyl-terminal domain repeat.The Journal of biological chemistry · 2013Article
- Studying protein complexes by the yeast two-hybrid system.Methods (San Diego, Calif.) · 2012Article
- Functional mammalian spliceosomal complex E contains SMN complex proteins in addition to U1 and U2 snRNPs.Nucleic acids research · 2012Article
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe FF domain is conserved across all eukaryotes and usually acts as an adaptor module in RNA metabolism and transcription. Saccharomyces cerevisiae encodes two FF domain proteins, Prp40, a component of the U1 snRNP, and Ypr152c, a protein of unknown function. The structure of Prp40, its relationship to other proteins within the U1 snRNP, and its precise function remain little understood.
resultsHere we have investigated the essentiality and interaction properties of the FF domains of yeast Prp40. We show that the C-terminal two FF domains of Prp40 are dispensable. Deletion of additional FF domains is lethal. The first FF domain of Prp40 binds to U1 protein Luc7 in yeast two-hybrid and GST pulldown experiments. FF domains 2 and 3 bind to Snu71, another known U1 protein. Peptide array screens identified binding sites for FF1-2 within Snu71 (NDVHY) and for FF1 within Luc7 (phi[FHL] x [KR] x [GHL] with phi being a hydrophobic amino acid).
conclusionPrp40, Luc7, and Snu71 appear to form a subcomplex within the yeast U1snRNP. Our data suggests that the N-terminal FF domains are critical for these interactions. Crystallization of Prp40, Luc7, and Snu71 have failed so far but co-crystallization of pairs or the whole tri-complex may facilitate crystallographic and further functional analysis.
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