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  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., 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.

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 Creators:
Wysoczanski, P.1, Author           
Schneider, C.2, Author           
Xiang, S. Q.3, Author           
Munari, F.1, Author           
Trowitzsch, S.2, Author           
Wahl, M. C., Author
Lührmann, R.2, Author           
Becker, S.4, Author           
Zweckstetter, M.1, Author           
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              
2Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578576              
3Research Group of Solid-State NMR, MPI for Biophysical Chemistry, Max Planck Society, ou_persistent35              
4Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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 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.

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Language(s): eng - English
 Dates: 2014-09-142014-10
 Publication Status: Issued
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 Rev. Type: Peer
 Identifiers: DOI: 10.1038/nsmb.2889
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Title: Nature Structural and Molecular Biology
Source Genre: Journal
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Pages: - Volume / Issue: 21 (10) Sequence Number: - Start / End Page: 911 - 918 Identifier: -