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4uqt

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Revision as of 11:11, 25 December 2014

RRM-peptide structure in RES complex

Structural highlights

4uqt is a 2 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
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 REtention and Splicing (RES) complex is a conserved spliceosome-associated module that was shown to enhance splicing of a subset of transcripts and to promote the nuclear retention of unspliced pre-mRNAs in yeast. The heterotrimeric RES complex is organized around the Snu17p protein that binds to both the Bud13p and Pml1p subunits. Snu17p exhibits an RRM domain that resembles a U2AF homology motif (UHM) and Bud13p harbors a Trp residue reminiscent of an UHM-ligand motif (ULM). It has therefore been proposed that the interaction between Snu17p and Bud13p resembles canonical UHM-ULM complexes. Here, we have used biochemical and NMR structural analysis to characterize the structure of the yeast Snu17p-Bud13p complex. Unlike known UHMs that sequester the Trp residue of the ULM ligand in a hydrophobic pocket, Snu17p and Bud13p utilize a large interaction surface formed around the two helices of the Snu17p domain. In total eighteen residues of Bud13p ligand wrap around the Snu17p helical surface in an U-turn-like arrangement. The invariant Trp232 in Bud13p is located in the center of the turn, and contacts surface residues of Snu17p. The structural data are supported by mutational analysis and indicate that the Snu17p provides an extended binding surface with Bud13p that is notably distinct from canonical UHM-ULM interactions. Our data highlight structural diversity in RNA recognition motif (RRM)-protein interactions, analogous to the one seen in for nucleic acid interactions.

A Novel Protein-Protein Interaction in the RES (REtention and Splicing) Complex.,Tripsianes K, Friberg A, Barrandon C, Brooks M, van Tilbeurgh H, Seraphin B, Sattler M J Biol Chem. 2014 Aug 26. pii: jbc.M114.592311. PMID:25160624^[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
↑ Tripsianes K, Friberg A, Barrandon C, Brooks M, van Tilbeurgh H, Seraphin B, Sattler M. A Novel Protein-Protein Interaction in the RES (REtention and Splicing) Complex. J Biol Chem. 2014 Aug 26. pii: jbc.M114.592311. PMID:25160624 doi:http://dx.doi.org/10.1074/jbc.M114.592311

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/4uqt"

@@ Line 5: / Line 5: @@
 </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=4uqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uqt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uqt RCSB], [http://www.ebi.ac.uk/pdbsum/4uqt 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 ==
@@ Line 17: / Line 19: @@
 __TOC__
 </StructureSection>
-[[Category: Barrandon, C.]]
+[[Category: Barrandon, C]]
-[[Category: Friberg, A.]]
+[[Category: Friberg, A]]
-[[Category: Sattler, M.]]
+[[Category: Sattler, M]]
-[[Category: Seraphin, B.]]
+[[Category: Seraphin, B]]
-[[Category: Tripsianes, K.]]
+[[Category: Tripsianes, K]]
 [[Category: Translation]]

4uqt

From Proteopedia

Revision as of 11:11, 25 December 2014

RRM-peptide structure in RES complex

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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