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Journal Article

Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex.

MPS-Authors
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Wysoczanski,  P.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

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Schneider,  C.
Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Xiang,  S. Q.
Research Group of Solid-State NMR, MPI for Biophysical Chemistry, Max Planck Society;

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Munari,  F.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

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Trowitzsch,  S.
Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Lührmann,  R.
Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Becker,  S.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Zweckstetter,  M.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

External Resource
Fulltext (public)

2069633.pdf
(Publisher version), 3MB

Supplementary Material (public)

2069633_Suppl.pdf
(Supplementary material), 3MB

Citation

Wysoczanski, P., Schneider, C., Xiang, S. Q., Munari, F., Trowitzsch, S., Wahl, M. C., et al. (2014). Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex. Nature Structural and Molecular Biology, 21(10), 911-918. doi:10.1038/nsmb.2889.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-26A6-0
Abstract
The precursor mRNA (pre-mRNA) retention and splicing (RES) complex is a spliceosomal complex that is present in yeast and humans and is important for RNA splicing and retention of unspliced pre-mRNA. Here, we present the solution NMR structure of the RES core complex from Saccharomyces cerevisiae. Complex formation leads to an intricate folding of three components-Snu17p, Bud13p and Pml1p-that stabilizes the RNA-recognition motif (RRM) fold of Snu17p and increases binding affinity in tertiary interactions between the components by more than 100-fold compared to that in binary interactions. RES interacts with pre-mRNA within the spliceosome, and through the assembly of the RES core complex RNA binding efficiency is increased. The three-dimensional structure of the RES core complex highlights the importance of cooperative folding and binding in the functional organization of the spliceosome.