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• W1909250875 abstract "Eukaryotic pre-mRNA splicing is catalysed by a large macromolecular complex called the spliceosome. One central unit of the spliceosome is the [U4/U6.U5] tri-snRNP particle that consists of the U4/U6 di-snRNP and the U5 snRNP mono-particle and is integrated into the spliceosome as a pre-assembled complex. During splicing dramatic structural rearrangements lead to the release of singular U4, U5 and U6 snRNP particle from the postspliceosomal complex. In order to take part in a new round of splicing the tri-snRNP particle has to be reformed from these singular components. Relatively little is known about the nuclear location at which the assembly of the tri-snRNP from U4/U6 di-snRNP and U5 mono-snRNP particle takes place. Candidates are subnuclear domains or regions such as the splice factor compartments (speckles), the Cajal bodies or the nucleoplasm. While the speckles very probably act as storage sites from which U snRNP particle and splicing factors can move to the sites of active splicing, a function of the Cajal bodies in assembly and maturation of de novo synthesized U snRNP particles was discussed.This work succeeded in identifying the site of tri-snRNP assembly in the nucleus by the development of a cellular system in which the [U4/U5.U6] tri-snRNP assembly in the cell was specifically blocked. For it the U4/U6-specific hPrp31 protein and the U5-specific hPrp6 protein were depleted from the cell by using RNA-Interference (RNAi). From both proteins it was known from in vitro studies that they form an essential connection between the U4/U6 di-snRNP and the U5 snRNP particle in the tri-snRNP particle. Biochemical characterization of hPrp31- and hPrp6 function in vivo using RNAi demonstrated that in the absence of protein hPrp31 or hPrp6 the tri-snRNP concentration in the cell was reduced whereas stable U4/U6 di-snRNP and U5 snRNP particle accumulated. Furthermore it was observed by fluorescence microscopy in cells that have been depleted from hPrp31 or hPrp6 protein that intact U4/U6 di-snRNP particle associated with p110 protein accumulate in Cajal bodies. In contrast to the situation observed for U4/U6 di-snRNP particle U5 snRNP mono-particle remain in the speckles.Protein p110 is required for di-snRNP formation and binds to both U6 (mono) snRNP and U4/U6 di-snRNP particle; and yet it is not a part of the tri-snRNP particle. As p110 protein has a Cajal body localisation signal the following model can be assumed for the final steps of [U4/U6.U5] tri-snRNP assembly in the Cajal bodies. Initially the U4/U6 di-snRNP particle is anchored to the Cajal body via its association with p110 protein. Then the U5 snRNP particle binds to the U4/U6 di-snRNP, with subsequent or concomitant dissociation or displacement of p110 and liberation of the mature [U4/U6.U5] tri-snRNP particle from the Cajal body.Additionally this work could demonstrate for the first time that the proteins hPrp31 and hPrp6 are imperative for cell viability and form an essential connection between the U4/U6 di-snRNP and the U5 mono-snRNP particle in the [U4/U6.U5] tri-snRNP particle in vivo. As a result of this the formation of the mature spliceosome from the pre-spliceosome is blocked in the absence of either of these proteins. This is of particular medical interest, because mutations in the hPrp31 coding gene are associated with autosomal dominant retinitis pigmentosa (adRP), a disease that leads to the degeneration of the photoreceptors in the eye." @default.
• W1909250875 created "2016-06-24" @default.
• W1909250875 creator A5024003910 @default.
• W1909250875 date "2022-02-16" @default.
• W1909250875 modified "2023-09-26" @default.
• W1909250875 title "Biochemische und zellbiologische Untersuchungen zur Rolle der Cajal Bodies bei der Zusammenlagerung spleißosomaler UsnRNP Partikel" @default.
• W1909250875 doi "https://doi.org/10.53846/goediss-111" @default.
• W1909250875 hasPublicationYear "2022" @default.
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