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| | ==Crystal structure of Saccharomyces cerevisiae RIF2== | | ==Crystal structure of Saccharomyces cerevisiae RIF2== |
| - | <StructureSection load='4bj1' size='340' side='right' caption='[[4bj1]], [[Resolution|resolution]] 2.94Å' scene=''> | + | <StructureSection load='4bj1' size='340' side='right'caption='[[4bj1]], [[Resolution|resolution]] 2.94Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4bj1]] is a 1 chain structure with sequence from [http://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=4BJ1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BJ1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4bj1]] is a 1 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=4BJ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BJ1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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]] 2.94Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4bj5|4bj5]], [[4bj6|4bj6]], [[4bjs|4bjs]], [[4bjt|4bjt]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=4bj1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bj1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bj1 RCSB], [http://www.ebi.ac.uk/pdbsum/4bj1 PDBsum]</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=4bj1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bj1 OCA], [https://pdbe.org/4bj1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bj1 RCSB], [https://www.ebi.ac.uk/pdbsum/4bj1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bj1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RIF2_YEAST RIF2_YEAST]] Involved in transcriptional silencing and telomere length regulation. Its role in telomere length regulation results from either a block in elongation or promoting degradation of the telomere ends. Loss of RIF1 function results in derepression of an HMR silencer, whose ARS consensus element has been deleted, and in the elongation of telomeres. RAP1 may target the binding of RIF1 to silencers and telomeres. | + | [https://www.uniprot.org/uniprot/RIF2_YEAST RIF2_YEAST] Involved in transcriptional silencing and telomere length regulation. Its role in telomere length regulation results from either a block in elongation or promoting degradation of the telomere ends. Loss of RIF1 function results in derepression of an HMR silencer, whose ARS consensus element has been deleted, and in the elongation of telomeres. RAP1 may target the binding of RIF1 to silencers and telomeres. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4bj1" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Saccharomyces cerevisiae s288c]] | + | [[Category: Large Structures]] |
| - | [[Category: Bunker, R D]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Gut, H]] | + | [[Category: Bunker RD]] |
| - | [[Category: Scrima, A]] | + | [[Category: Gut H]] |
| - | [[Category: Shi, T]] | + | [[Category: Scrima A]] |
| - | [[Category: Thoma, N H]] | + | [[Category: Shi T]] |
| - | [[Category: Aaa+ fold]]
| + | [[Category: Thoma NH]] |
| - | [[Category: Dna binding protein]]
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| - | [[Category: Genome stability]]
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| - | [[Category: Telomere associated protein]]
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| Structural highlights
Function
RIF2_YEAST Involved in transcriptional silencing and telomere length regulation. Its role in telomere length regulation results from either a block in elongation or promoting degradation of the telomere ends. Loss of RIF1 function results in derepression of an HMR silencer, whose ARS consensus element has been deleted, and in the elongation of telomeres. RAP1 may target the binding of RIF1 to silencers and telomeres.
Publication Abstract from PubMed
Yeast telomeres comprise irregular TG1-3 DNA repeats bound by the general transcription factor Rap1. Rif1 and Rif2, along with Rap1, form the telosome, a protective cap that inhibits telomerase, counteracts SIR-mediated transcriptional silencing, and prevents inadvertent recognition of telomeres as DNA double-strand breaks. We provide a molecular, biochemical, and functional dissection of the protein backbone at the core of the yeast telosome. The X-ray structures of Rif1 and Rif2 bound to the Rap1 C-terminal domain and that of the Rif1 C terminus are presented. Both Rif1 and Rif2 have separable and independent Rap1-binding epitopes, allowing Rap1 binding over large distances (42-110 A). We identify tetramerization (Rif1) and polymerization (Rif2) modules that, in conjunction with the long-range binding, give rise to a higher-order architecture that interlinks Rap1 units. This molecular Velcro relies on Rif1 and Rif2 to recruit and stabilize Rap1 on telomeric arrays and is required for telomere homeostasis in vivo.
Rif1 and Rif2 Shape Telomere Function and Architecture through Multivalent Rap1 Interactions.,Shi T, Bunker RD, Mattarocci S, Ribeyre C, Faty M, Gut H, Scrima A, Rass U, Rubin SM, Shore D, Thoma NH Cell. 2013 Jun 6;153(6):1340-53. doi: 10.1016/j.cell.2013.05.007. PMID:23746845[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Shi T, Bunker RD, Mattarocci S, Ribeyre C, Faty M, Gut H, Scrima A, Rass U, Rubin SM, Shore D, Thoma NH. Rif1 and Rif2 Shape Telomere Function and Architecture through Multivalent Rap1 Interactions. Cell. 2013 Jun 6;153(6):1340-53. doi: 10.1016/j.cell.2013.05.007. PMID:23746845 doi:10.1016/j.cell.2013.05.007
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