The Role of the U5 snRNP in Genetic Disorders and Cancer [PDF]
Pre-mRNA splicing is performed by the spliceosome, a dynamic macromolecular complex consisting of five small uridine-rich ribonucleoprotein complexes (the U1, U2, U4, U5, and U6 snRNPs) and numerous auxiliary splicing factors.
Katherine A. Wood +5 more
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TSSC4 is a component of U5 snRNP that promotes tri-snRNP formation [PDF]
The correct assembly and recycling of the multicomponent spliceosome remains largely elusive. Here, the authors show that a previously uncharacterized protein TSSC4 associates with de novo formed spliceosomal U5 snRNP as well as with a post-splicing U5 ...
Klára Klimešová +6 more
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U5 snRNP Core Proteins Are Key Components of the Defense Response against Viral Infection through Their Roles in Programmed Cell Death and Interferon Induction [PDF]
The spliceosome is a massive ribonucleoprotein structure composed of five small nuclear ribonucleoprotein (snRNP) complexes that catalyze the removal of introns from pre-mature RNA during constitutive and alternative splicing. EFTUD2, PRPF8, and SNRNP200
Simon Boudreault +2 more
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Addressing the tissue specificity of U5 snRNP spliceosomopathies [PDF]
Precursor mRNA (pre-mRNA) must undergo splicing to remove intron sequences and join exons. This splicing process is catalysed by an RNA/protein complex called the spliceosome.
Rahmat Azhari Kemal +2 more
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The 35S U5 snRNP Is Generated from the Activated Spliceosome during In vitro Splicing. [PDF]
Primary gene transcripts of eukaryotes contain introns, which are removed during processing by splicing machinery. Biochemical studies In vitro have identified a specific pathway in which introns are recognised and spliced out. This occurs by progressive
Olga V Makarova, Evgeny M Makarov
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Cell cycle abnormalities associated with differential perturbations of the human U5 snRNP associated U5-200kD RNA helicase. [PDF]
Splicing of pre-messenger RNAs into functional messages requires a concerted assembly of proteins and small RNAs that identify the splice junctions and facilitate cleavage of exon-intron boundaries and ligation of exons.
Ali Ehsani +2 more
doaj +3 more sources
Reovirus μ2 protein modulates host cell alternative splicing by reducing protein levels of U5 snRNP core components. [PDF]
Mammalian orthoreovirus (MRV) is a double-stranded RNA virus from the Reoviridae family presenting a promising activity as an oncolytic virus. Recent studies have underlined MRV’s ability to alter cellular alternative splicing (AS) during infection, with
Boudreault S +5 more
europepmc +2 more sources
Reovirus μ2 Protein Impairs Translation to Reduce U5 snRNP Protein Levels. [PDF]
Mammalian orthoreovirus (MRV) is a double-stranded RNA virus from the Reoviridae family that infects a large range of mammals, including humans. Recently, studies have shown that MRV alters cellular alternative splicing (AS) during viral infection.
Boudreault S +5 more
europepmc +2 more sources
Ecd promotes U5 snRNP maturation and Prp8 stability. [PDF]
Pre-mRNA splicing catalyzed by the spliceosome represents a critical step in the regulation of gene expression contributing to transcriptome and proteome diversity.
Erkelenz S +7 more
europepmc +2 more sources
Structure of the human 20S U5 snRNP. [PDF]
The 20S U5 small nuclear ribonucleoprotein particle (snRNP) is a 17-subunit RNA–protein complex and a precursor of the U4/U6.U5 tri-snRNP, the major building block of the precatalytic spliceosome.
Schneider S +8 more
europepmc +2 more sources

