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

Wysoczanski, P.; Schneider, C.; Xiang, S. Q.; Munari, F.; Trowitzsch, S.; Wahl, M. C.; Lührmann, R.; Becker, S.; Zweckstetter, M.

doi:10.1038/nsmb.2889

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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;

/persons/resource/persons135772

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

/persons/resource/persons86706

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

/persons/resource/persons71698

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

/persons/resource/persons59291

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

/persons/resource/persons15470

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

/persons/resource/persons14824

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

/persons/resource/persons16093

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

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2069633_Suppl.pdf
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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: https://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.