2mkc

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Cooperative Structure of the Heterotrimeric pre-mRNA Retention and Splicing ComplexCooperative Structure of the Heterotrimeric pre-mRNA Retention and Splicing Complex

Structural highlights

2mkc is a 3 chain structure with sequence from Saccharomyces cerevisiae S288C. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

IST3_YEAST Required for pre-mRNA splicing and spliceosome assembly. As part of the pre-mRNA retention and splicing (RES) complex, required for nuclear pre-mRNA retention and efficient splicing. Required for MER1-activated splicing.[1] [2] [3]

Publication Abstract from PubMed

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.

Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex.,Wysoczanski P, Schneider C, Xiang S, Munari F, Trowitzsch S, Wahl MC, Luhrmann R, Becker S, Zweckstetter M Nat Struct Mol Biol. 2014 Sep 14. doi: 10.1038/nsmb.2889. PMID:25218446[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Gottschalk A, Bartels C, Neubauer G, Luhrmann R, Fabrizio P. A novel yeast U2 snRNP protein, Snu17p, is required for the first catalytic step of splicing and for progression of spliceosome assembly. Mol Cell Biol. 2001 May;21(9):3037-46. PMID:11287609 doi:http://dx.doi.org/10.1128/MCB.21.9.3037-3046.2001
  2. Dziembowski A, Ventura AP, Rutz B, Caspary F, Faux C, Halgand F, Laprevote O, Seraphin B. Proteomic analysis identifies a new complex required for nuclear pre-mRNA retention and splicing. EMBO J. 2004 Dec 8;23(24):4847-56. Epub 2004 Nov 25. PMID:15565172 doi:http://dx.doi.org/7600482
  3. Spingola M, Armisen J, Ares M Jr. Mer1p is a modular splicing factor whose function depends on the conserved U2 snRNP protein Snu17p. Nucleic Acids Res. 2004 Feb 18;32(3):1242-50. Print 2004. PMID:14973223 doi:http://dx.doi.org/10.1093/nar/gkh281
  4. Wysoczanski P, Schneider C, Xiang S, Munari F, Trowitzsch S, Wahl MC, Luhrmann R, Becker S, Zweckstetter M. Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex. Nat Struct Mol Biol. 2014 Sep 14. doi: 10.1038/nsmb.2889. PMID:25218446 doi:http://dx.doi.org/10.1038/nsmb.2889
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