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| | <StructureSection load='5v1a' size='340' side='right'caption='[[5v1a]], [[Resolution|resolution]] 2.14Å' scene=''> | | <StructureSection load='5v1a' size='340' side='right'caption='[[5v1a]], [[Resolution|resolution]] 2.14Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5v1a]] 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=5V1A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5V1A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5v1a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V1A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5V1A FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ULP2, SMT4, YIL031W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), CSM1, SPO86, YCR086W, YCR86W ([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]] 2.14Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ulp1_peptidase Ulp1 peptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.68 3.4.22.68] </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=5v1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v1a OCA], [https://pdbe.org/5v1a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5v1a RCSB], [https://www.ebi.ac.uk/pdbsum/5v1a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5v1a ProSAT]</span></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=5v1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v1a OCA], [http://pdbe.org/5v1a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5v1a RCSB], [http://www.ebi.ac.uk/pdbsum/5v1a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5v1a ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ULP2_YEAST ULP2_YEAST]] Insertion mutation in SMT4 confers temperature and benomyl sensitivity; high copy suppressor of a temperature sensitive mutation in MIF2. [[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/ULP2_YEAST ULP2_YEAST] Insertion mutation in SMT4 confers temperature and benomyl sensitivity; high copy suppressor of a temperature sensitive mutation in MIF2. |
| | <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: Ulp1 peptidase]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Corbett, K D]] | + | [[Category: Corbett KD]] |
| - | [[Category: Singh, N]] | + | [[Category: Singh N]] |
| - | [[Category: Cohibin]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Monopolin]]
| + | |
| - | [[Category: Rdna silencing]]
| + | |
| - | [[Category: Sumo isopeptidase]]
| + | |
| Structural highlights
Function
ULP2_YEAST Insertion mutation in SMT4 confers temperature and benomyl sensitivity; high copy suppressor of a temperature sensitive mutation in MIF2.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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
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