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ID: 16683.0, MPI für biophysikalische Chemie / Zelluläre Biochemie (Prof. Reinhard Lührmann)
Hierarchical, clustered protein interact ions with U4/U6 snRNA: a biochemical role for U4/U6 proteins
Authors:Nottrott, S.; Urlaub, H.; Luehrmann, R.
Date of Publication (YYYY-MM-DD):2002-10-15
Title of Journal:EMBO Journal
Issue / Number:20
Start Page:5527
End Page:5538
Review Status:Peer-review
Audience:Not Specified
Abstract / Description:During activation of the spliceosome,, the U4/U6 snRNA duplex is dissociated, releasing U6 for subsequent base pairing with U2 snRNA. Proteins that directly bind the U4/U6 interaction domain potentially could mediate these structural changes. We thus investigated binding of the human U4/U6-specific proteins, 15.5K, 61K and the 20/60/90K protein complex, to U4/U6 snRNA in vitro. We demonstrate that protein 15.5K is a nucleation factor for U4/U6 snRNP assembly, mediating the interaction of 61K and 20/60/90K with U4/U6 snRNA. A similar hierarchical assembly pathway is observed for the U4atac/U6atac snRNP. In addition, we show that protein 61K directly contacts the 5' portion of U4 snRNA via a novel RNA-binding domain. Furthermore, the 20/60/90K heteromer requires stem II but not stem I of the U4/U6 duplex for binding, and this interaction involves a direct contact between protein 90K and U6. This uneven clustering of the U4/U6 snRNP-specific proteins on U4/U6 snRNA is consistent with a sequential dissociation of the U4/U6 duplex prior to spliceosome catalysis.
Free Keywords:pre-mRNA splicing; protein-RNA interaction; protein 15.5K; RNA- binding domain; snRNP assembly
Comment of the Author/Creator:Date: 2002, OCT 15
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für biophysikalische Chemie/Abt. Reinhard Lührmann / 100
MPI für biophysikalische Chemie/AG Henning Urlaub
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