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5v3n

From Proteopedia

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Structure of S. cerevisiae Ulp2-Tof2-Csm1 complex

Structural highlights

5v3n is a 2 chain structure with sequence from Saccharomyces cerevisiae S288C and Saccharomyces cerevisiae x Saccharomyces kudriavzevii VIN7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.3Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CSM1_YEAST Component of the monopolin complex which promotes monoorientation during meiosis I, required for chromosome segregation during meiosis. Plays also a mitotic role in DNA replication.^[1] ^[2] ^[3] ^[4] ^[5]

Publication Abstract from PubMed

Post-translational modification by SUMO (small ubiquitin-like modifier) plays important but still poorly understood regulatory roles in eukaryotic cells, including as a signal for ubiquitination by SUMO targeted ubiquitin ligases (STUbLs). Here, we delineate the molecular mechanisms for SUMO-dependent control of ribosomal DNA (rDNA) silencing through the opposing actions of a STUbL (Slx5:Slx8) and a SUMO isopeptidase (Ulp2). We identify a conserved region in the Ulp2 C terminus that mediates its specificity for rDNA-associated proteins and show that this region binds directly to the rDNA-associated protein Csm1. Two crystal structures show that Csm1 interacts with Ulp2 and one of its substrates, the rDNA silencing protein Tof2, through adjacent conserved interfaces in its C-terminal domain. Disrupting Csm1's interaction with either Ulp2 or Tof2 dramatically reduces rDNA silencing and causes a marked drop in Tof2 abundance, suggesting that Ulp2 promotes rDNA silencing by opposing STUbL-mediated degradation of silencing proteins. Tof2 abundance is rescued by deletion of the STUbL SLX5 or disruption of its SUMO-interacting motifs, confirming that Tof2 is targeted for degradation in a SUMO- and STUbL-dependent manner. Overall, our results demonstrate how the opposing actions of a localized SUMO isopeptidase and a STUbL regulate rDNA silencing by controlling the abundance of a key rDNA silencing protein, Tof2.

Recruitment of a SUMO isopeptidase to rDNA stabilizes silencing complexes by opposing SUMO targeted ubiquitin ligase activity.,Liang J, Singh N, Carlson CR, Albuquerque CP, Corbett KD, Zhou H Genes Dev. 2017 Apr 15;31(8):802-815. doi: 10.1101/gad.296145.117. Epub 2017 May , 9. PMID:28487408^[6]

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

References

↑ Rabitsch KP, Toth A, Galova M, Schleiffer A, Schaffner G, Aigner E, Rupp C, Penkner AM, Moreno-Borchart AC, Primig M, Esposito RE, Klein F, Knop M, Nasmyth K. A screen for genes required for meiosis and spore formation based on whole-genome expression. Curr Biol. 2001 Jul 10;11(13):1001-9. PMID:11470404
↑ Rabitsch KP, Petronczki M, Javerzat JP, Genier S, Chwalla B, Schleiffer A, Tanaka TU, Nasmyth K. Kinetochore recruitment of two nucleolar proteins is required for homolog segregation in meiosis I. Dev Cell. 2003 Apr;4(4):535-48. PMID:12689592
↑ Wysocka M, Rytka J, Kurlandzka A. Saccharomyces cerevisiae CSM1 gene encoding a protein influencing chromosome segregation in meiosis I interacts with elements of the DNA replication complex. Exp Cell Res. 2004 Apr 1;294(2):592-602. PMID:15023545 doi:10.1016/j.yexcr.2003.12.008
↑ Pan X, Ye P, Yuan DS, Wang X, Bader JS, Boeke JD. A DNA integrity network in the yeast Saccharomyces cerevisiae. Cell. 2006 Mar 10;124(5):1069-81. Epub 2006 Feb 16. PMID:16487579 doi:S0092-8674(06)00118-8
↑ Mekhail K, Seebacher J, Gygi SP, Moazed D. Role for perinuclear chromosome tethering in maintenance of genome stability. Nature. 2008 Dec 4;456(7222):667-70. doi: 10.1038/nature07460. Epub 2008 Nov 9. PMID:18997772 doi:10.1038/nature07460
↑ Liang J, Singh N, Carlson CR, Albuquerque CP, Corbett KD, Zhou H. Recruitment of a SUMO isopeptidase to rDNA stabilizes silencing complexes by opposing SUMO targeted ubiquitin ligase activity. Genes Dev. 2017 Apr 15;31(8):802-815. doi: 10.1101/gad.296145.117. Epub 2017 May , 9. PMID:28487408 doi:http://dx.doi.org/10.1101/gad.296145.117

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/5v3n"

Categories: Large Structures | Saccharomyces cerevisiae S288C | Saccharomyces cerevisiae x Saccharomyces kudriavzevii VIN7 | Corbett KD | SIngh N

@@ Line 3: / Line 3: @@
 <StructureSection load='5v3n' size='340' side='right'caption='[[5v3n]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5v3n]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V3N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5V3N FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5v3n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_x_Saccharomyces_kudriavzevii_VIN7 Saccharomyces cerevisiae x Saccharomyces kudriavzevii VIN7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V3N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5V3N FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CSM1, SPO86, YCR086W, YCR86W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), TOF2, YKR010C, YK109 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</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=5v3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v3n OCA], [http://pdbe.org/5v3n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5v3n RCSB], [http://www.ebi.ac.uk/pdbsum/5v3n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5v3n ProSAT]</span></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=5v3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v3n OCA], [https://pdbe.org/5v3n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5v3n RCSB], [https://www.ebi.ac.uk/pdbsum/5v3n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5v3n ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CSM1_YEAST CSM1_YEAST]] Component of the monopolin complex which promotes monoorientation during meiosis I, required for chromosome segregation during meiosis. Plays also a mitotic role in DNA replication.<ref>PMID:11470404</ref> <ref>PMID:12689592</ref> <ref>PMID:15023545</ref> <ref>PMID:16487579</ref> <ref>PMID:18997772</ref>
+[https://www.uniprot.org/uniprot/CSM1_YEAST CSM1_YEAST] Component of the monopolin complex which promotes monoorientation during meiosis I, required for chromosome segregation during meiosis. Plays also a mitotic role in DNA replication.<ref>PMID:11470404</ref> <ref>PMID:12689592</ref> <ref>PMID:15023545</ref> <ref>PMID:16487579</ref> <ref>PMID:18997772</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Baker's yeast]]
 [[Category: Large Structures]]
-[[Category: Corbett, K D]]
+[[Category: Saccharomyces cerevisiae S288C]]
-[[Category: SIngh, N]]
+[[Category: Saccharomyces cerevisiae x Saccharomyces kudriavzevii VIN7]]
-[[Category: Cohibin]]
+[[Category: Corbett KD]]
-[[Category: Desumoylation]]
+[[Category: SIngh N]]
-[[Category: Hydrolase]]
-[[Category: Monopolin]]
-[[Category: Rdna silencing]]

5v3n

From Proteopedia

Current revision

Structure of S. cerevisiae Ulp2-Tof2-Csm1 complex

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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