New insights into trypanosomatid U5 small nuclear ribonucleoproteins
Memorias do Instituto Oswaldo Cruz, 2011 Several protozoan parasites exist in the Trypanosomatidae family, including various agents of human diseases. Multiple lines of evidence suggest that important differences are present between the translational and mRNA processing (trans splicing) systems
Marco Túlio A da Silva +8 more
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A sart1 Zebrafish Mutant Results in Developmental Defects in the Central Nervous System
Cells, 2020 The spliceosome consists of accessory proteins and small nuclear ribonucleoproteins (snRNPs) that remove introns from RNA. As splicing defects are associated with degenerative conditions, a better understanding of spliceosome formation and function is ...
Hannah E. Henson, Michael R. Taylor
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Breaking up the C complex spliceosome shows stable association of proteins with the lariat intron intermediate. [PDF]
PLoS ONE, 2011 Spliceosome assembly requires several structural rearrangements to position the components of the catalytic core. Many of these rearrangements involve successive strengthening and weakening of different RNA:RNA and RNA:proteins interactions within the ...
Patricia Coltri +4 more
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Identification of an RNA-Dependent ATPase Activity in Mammalian U5 snRNPs [PDF]
Nucleic Acids Research, 1996 Nuclear pre-mRNA splicing requires ATP at several steps from spliceosome assembly to product release. Here, we demonstrate that an integral component of the 20S U5 snRNP is an RNA-dependent ATPase. The ATPase activity of 20S U5 and 25S [U4/U6.U5] snRNPs purified by glycerol gradient centrifugation is strongly stimulated by homopolymeric RNA but not ...
B, Laggerbauer, J, Lauber, R, Lührmann
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A novel RNA-binding activity of ECD contributes to U5 snRNP stability and pre-mRNA splicing
bioRxivHuman ecdysoneless protein (ECD) plays an essential role in regulating cell cycle progression and cell survival. ECD has previously been implicated in RNA splicing through its association with spliceosomal proteins.
M. Raza +9 more
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eLife, 2015 Prp3 is an essential U4/U6 di-snRNP-associated protein whose functions and molecular mechanisms in pre-mRNA splicing are presently poorly understood. We show by structural and biochemical analyses that Prp3 contains a bipartite U4/U6 di-snRNA-binding ...
Sunbin Liu +9 more
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U4/U5/U6 snRNP recognizes the 5' splice site in the absence of U2 snRNP. [PDF]
Genes & Development, 1994 Using an in vitro system in which a 5' splice site (5'SS) RNA oligo (AAG decreases GUAAGUAdT) is capable of inducing formation of U2/U4/U5/U6 snRNP complex we show that this oligo specifically binds to U4/U5/U6 snRNP and cross-links to U6 snRNA in the absence of U2 snRNP.
B B, Konforti, M M, Konarska
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Antisense oligonucleotide binding to U5 snRNP induces a conformational change that exposes the conserved loop of U5 snRNA [PDF]
Nucleic Acids Research, 1997 Conformational rearrangements of the spliceosomal small nuclear RNAs (U snRNAs) are essential for proper assembly of the active site prior to the first catalytic step of splicing. We have previously shown that conformational changes caused by binding of an antisense 2'-O-methyl RNA oligonucleotide (BU5Ae) to U5 snRNA nt 68-88 disrupted the U4/U5/U6 ...
G, Ast, A M, Weiner
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In vitro reconstitution of mammalian U2 and U5 snRNPs active in splicing: Sm proteins are functionally interchangeable and are essential for the formation of functional U2 and U5 snRNPs. [PDF]
The EMBO Journal, 1995 An in vitro reconstitution/splicing complementation system has been developed which has allowed the investigation of the role of mammalian U2 and U5 snRNP components in splicing. U2 or U5 snRNP cores are first reconstituted from purified native snRNP core proteins and snRNA in the absence of cellular extract and are subsequently added to splicing ...
V, Ségault +3 more
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Single molecule analysis reveals reversible and irreversible steps during spliceosome activation
eLife, 2016 The spliceosome is a complex machine composed of small nuclear ribonucleoproteins (snRNPs) and accessory proteins that excises introns from pre-mRNAs.
Aaron A Hoskins +4 more
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