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  Stable tri-snRNP integration is accompanied by a major structural rearrangement of the spliceosome that is dependent on Prp8 interaction with the 5‘ splice site.

Boesler, C., Rigo, N., Agafonov, D. E., Kastner, B., Urlaub, H., Will, C. L., et al. (2015). Stable tri-snRNP integration is accompanied by a major structural rearrangement of the spliceosome that is dependent on Prp8 interaction with the 5‘ splice site. RNA, 21(11), 1993-2005. doi:10.1261/rna.053991.115.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-4609-E Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-5CD4-5
Genre: Journal Article

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 Creators:
Boesler, C.1, Author              
Rigo, N.1, Author              
Agafonov, D. E.1, Author              
Kastner, B.1, Author              
Urlaub, H.2, Author              
Will, C. L.1, Author              
Lührmann, R.1, Author              
Affiliations:
1Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578576              
2Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              

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Free keywords: pre-mRNA splicing, spliceosome, exon definition, tri-snRNP, Prp8
 Abstract: Exon definition is the predominant initial spliceosome assembly pathway in higher eukaryotes, but it remains much less well-characterized compared to the intron-defined assembly pathway. Addition in trans of an excess of 5′ss containing RNA to a splicing reaction converts a 37S exon-defined complex, formed on a single exon RNA substrate, into a 45S B-like spliceosomal complex with stably integrated U4/U6.U5 tri-snRNP. This 45S complex is compositonally and structurally highly similar to an intron-defined spliceosomal B complex. Stable tri-snRNP integration during B-like complex formation is accompanied by a major structural change as visualized by electron microscopy. The changes in structure and stability during transition from a 37S to 45S complex can be induced in affinity-purified cross-exon complexes by adding solely the 5′ss RNA oligonucleotide. This conformational change does not require the B-specific proteins, which are recruited during this stabilization process, or site-specific phosphorylation of hPrp31. Instead it is triggered by the interaction of U4/U6.U5 tri-snRNP components with the 5′ss sequence, most importantly between Prp8 and nucleotides at the exon–intron junction. These studies provide novel insights into the conversion of a cross-exon to cross-intron organized spliceosome and also shed light on the requirements for stable tri-snRNP integration during B complex formation.

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Language(s): eng - English
 Dates: 2015-09-18
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1261/rna.053991.115
 Degree: -

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Title: RNA
Source Genre: Journal
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Pages: - Volume / Issue: 21 (11) Sequence Number: - Start / End Page: 1993 - 2005 Identifier: -