ArticleThe Biochemical journal2017
The spliceosomal proteins PPIH and PRPF4 exhibit bi-partite binding.
Article in The Biochemical journal, 2017. 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.
- A non-catalytic interaction surface mediates recognition of spliceosomal factors by the Toxoplasma gondii cyclophilin TgCyp23.The Biochemical journal · 2026Article
- Human Cyclophilins-An Emerging Class of Drug Targets.Medicinal research reviews · 2026Review
- Alternative Splicing Dysregulation in Retinitis Pigmentosa: Pathogenic Mechanisms and Therapeutic Opportunities.Biomolecules · 2025Review
- PPIH is a novel diagnostic biomarker associated with immune infiltration in cholangiocarcinoma.BMC cancer · 2025Article
- eQTL and multi-omics integration reveal PPIH as a prognostic and immunotherapeutic biomarker.Frontiers in immunology · 2025Article
- PPIH acts as a potential predictive biomarker for patients with common solid tumors.BMC cancer · 2024Article
- Article
- Transcriptome-wide association study uncovers the role of essential genes in anthracycline-induced cardiotoxicity.NPJ genomic medicine · 2021Article
- Fast mutual exclusivity algorithm nominates potential synthetic lethal gene pairs through brute force matrix product computations.Computational and structural biotechnology journal · 2021Article
- Structural and Functional Insights into Human Nuclear Cyclophilins.Biomolecules · 2018Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Pre-mRNA splicing is a dynamic, multistep process that is catalyzed by the RNA (ribonucleic acid)-protein complex called the spliceosome. The spliceosome contains a core set of RNAs and proteins that are conserved in all organisms that perform splicing. In higher organisms, peptidyl-prolyl isomerase H (PPIH) directly interacts with the core protein pre-mRNA processing factor 4 (PRPF4) and both integrate into the pre-catalytic spliceosome as part of the tri-snRNP (small nuclear RNA-protein complex) subcomplex. As a first step to understand the protein interactions that dictate PPIH and PRPF4 function, we expressed and purified soluble forms of each protein and formed a complex between them. We found two sites of interaction between PPIH and the N-terminus of PRPF4, an unexpected result. The N-terminus of PRPF4 is an intrinsically disordered region and does not adopt secondary structure in the presence of PPIH. In the absence of an atomic resolution structure, we used mutational analysis to identify point mutations that uncouple these two binding sites and find that mutations in both sites are necessary to break up the complex. A discussion of how this bipartite interaction between PPIH and PRPF4 may modulate spliceosomal function is included.
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Registered trials
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.