2my2

From Proteopedia

(Difference between revisions)

Revision as of 14:40, 12 August 2015

Snu17p-Bud13p structure intermediate during RES complex assembly

Structural highlights

2my2 is a 2 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2mkc, 2my3
Resources:	FirstGlance, OCA, RCSB, PDBsum

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] [CWC26_YEAST] Required for efficient splicing and pre-mRNA nuclear retention. May also be involved in positioning the proximal bud pole signal.^[4] ^[5] ^[6] ^[7]

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^[8]

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

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
↑ Zahner JE, Harkins HA, Pringle JR. Genetic analysis of the bipolar pattern of bud site selection in the yeast Saccharomyces cerevisiae. Mol Cell Biol. 1996 Apr;16(4):1857-70. PMID:8657162
↑ Ni L, Snyder M. A genomic study of the bipolar bud site selection pattern in Saccharomyces cerevisiae. Mol Biol Cell. 2001 Jul;12(7):2147-70. PMID:11452010
↑ Vincent K, Wang Q, Jay S, Hobbs K, Rymond BC. Genetic interactions with CLF1 identify additional pre-mRNA splicing factors and a link between activators of yeast vesicular transport and splicing. Genetics. 2003 Jul;164(3):895-907. PMID:12871902
↑ 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
↑ 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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2my2"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==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=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2my2]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MY2 FirstGlance]. <br>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2mkc|2mkc]], [[2my3|2my3]]</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2my2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2my2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2my2 RCSB], [http://www.ebi.ac.uk/pdbsum/2my2 PDBsum]</span></td></tr>
+</table>
+== Function ==
+[[http://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>  [[http://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>
+<div style="background-color:#fffaf0;">
+== 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.
-The entry 2my2 is ON HOLD  until Paper Publication
+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<ref>PMID:26212312</ref>
-Authors: Wysoczanski, P., Becker, S., Zweckstetter, M.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Snu17p-Bud13p structure intermediate during RES complex assembly
+== References ==
-[[Category: Unreleased Structures]]
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Becker, S]]
+[[Category: Wysoczanski, P]]
 [[Category: Zweckstetter, M]]
-[[Category: Wysoczanski, P]]
+[[Category: Cooperativity]]
+[[Category: Heterodimer]]
+[[Category: Ist3p]]
+[[Category: Pml1p]]
+[[Category: Re]]
+[[Category: Rrm]]
+[[Category: Snu17p]]
+[[Category: Spliceosome]]
+[[Category: Splicing]]

2my2

From Proteopedia

Revision as of 14:40, 12 August 2015

Snu17p-Bud13p structure intermediate during RES complex assembly

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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