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| | ==Snu17p-Bud13p structure intermediate during RES complex assembly== | | ==Snu17p-Bud13p structure intermediate during RES complex assembly== |
| - | <StructureSection load='2my2' size='340' side='right'caption='[[2my2]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2my2' size='340' side='right'caption='[[2my2]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2my2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MY2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2my2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MY2 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2mkc|2mkc]], [[2my3|2my3]]</div></td></tr> | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2my2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2my2 OCA], [https://pdbe.org/2my2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2my2 RCSB], [https://www.ebi.ac.uk/pdbsum/2my2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2my2 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IST3, SNU17, YIB5W, YIR005W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), BUD13, CWC26, G1642, SLC7, YGL174W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2my2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2my2 OCA], [https://pdbe.org/2my2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2my2 RCSB], [https://www.ebi.ac.uk/pdbsum/2my2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2my2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/IST3_YEAST 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.<ref>PMID:11287609</ref> <ref>PMID:15565172</ref> <ref>PMID:14973223</ref> [[https://www.uniprot.org/uniprot/CWC26_YEAST CWC26_YEAST]] Required for efficient splicing and pre-mRNA nuclear retention. May also be involved in positioning the proximal bud pole signal.<ref>PMID:8657162</ref> <ref>PMID:11452010</ref> <ref>PMID:12871902</ref> <ref>PMID:15565172</ref>
| + | [https://www.uniprot.org/uniprot/IST3_YEAST 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.<ref>PMID:11287609</ref> <ref>PMID:15565172</ref> <ref>PMID:14973223</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Baker's yeast]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Becker, S]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Wysoczanski, P]] | + | [[Category: Becker S]] |
| - | [[Category: Zweckstetter, M]] | + | [[Category: Wysoczanski P]] |
| - | [[Category: Cooperativity]] | + | [[Category: Zweckstetter M]] |
| - | [[Category: Heterodimer]]
| + | |
| - | [[Category: Ist3p]]
| + | |
| - | [[Category: Pml1p]]
| + | |
| - | [[Category: Re]]
| + | |
| - | [[Category: Rrm]]
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| - | [[Category: Snu17p]]
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| - | [[Category: Spliceosome]]
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| - | [[Category: Splicing]]
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| Structural highlights
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 action of the spliceosome depends on the stepwise cooperative assembly and disassembly of its components. Very strong cooperativity was observed for the RES (Retention and Splicing) hetero-trimeric complex where the affinity from binary to tertiary interactions changes more than 100-fold and affects RNA binding. The RES complex is involved in splicing regulation and retention of not properly spliced pre-mRNA with its three components-Snu17p, Pml1p and Bud13p-giving rise to the two possible intermediate dimeric complexes Pml1p-Snu17p and Bud13p-Snu17p. Here we determined the three-dimensional structure and dynamics of the Pml1p-Snu17p and Bud13p-Snu17p dimers using liquid state NMR. We demonstrate that localized as well as global changes occur along the RES trimer assembly pathway. The stepwise rigidification of the Snu17p structure following the binding of Pml1p and Bud13p provides a basis for the strong cooperative nature of RES complex assembly.
Structures of intermediates during RES complex assembly.,Wysoczanski P, Becker S, Zweckstetter M Sci Rep. 2015 Jul 27;5:12545. doi: 10.1038/srep12545. PMID:26212312[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ Wysoczanski P, Becker S, Zweckstetter M. Structures of intermediates during RES complex assembly. Sci Rep. 2015 Jul 27;5:12545. doi: 10.1038/srep12545. PMID:26212312 doi:http://dx.doi.org/10.1038/srep12545
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