4bjs

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<StructureSection load='4bjs' size='340' side='right'caption='[[4bjs]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
<StructureSection load='4bjs' size='340' side='right'caption='[[4bjs]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4bjs]] is a 4 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=4BJS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BJS FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4bjs]] is a 4 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=4BJS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BJS FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4bj1|4bj1]], [[4bj5|4bj5]], [[4bj6|4bj6]], [[4bjt|4bjt]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.94&#8491;</td></tr>
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<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=4bjs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bjs OCA], [http://pdbe.org/4bjs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bjs RCSB], [http://www.ebi.ac.uk/pdbsum/4bjs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bjs ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4bjs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bjs OCA], [https://pdbe.org/4bjs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bjs RCSB], [https://www.ebi.ac.uk/pdbsum/4bjs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bjs ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/RIF1_YEAST RIF1_YEAST]] Negatively regulates telomere length by preventing telomere elongation or promoting degradation of the telomere ends. Recruited to telomeres by interaction with the C-terminus of RAP1, which binds directly to telomeric repeat DNA. This may create a negative feedback loop in which the addition of new telomere repeats creates binding sites for inhibitors of telomere length extension. May also influence the balance of transcriptional silencing at telomeres and the silent mating type locus HMR, which is mediated by SIR (Silent Information Regulator) proteins including SIR3 and SIR4. RIF1 competes with SIR proteins for binding to the C-terminus of RAP1. In the absence of RIF1, a limiting cellular pool of SIR proteins may preferentially associate with RAP1 at sub-telomeric loci, causing enhanced telomeric silencing and attenuated silencing of the HMR locus.<ref>PMID:1577274</ref> <ref>PMID:7867933</ref> <ref>PMID:9087429</ref> <ref>PMID:10531008</ref> <ref>PMID:15572688</ref>
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[https://www.uniprot.org/uniprot/RIF1_YEAST RIF1_YEAST] Negatively regulates telomere length by preventing telomere elongation or promoting degradation of the telomere ends. Recruited to telomeres by interaction with the C-terminus of RAP1, which binds directly to telomeric repeat DNA. This may create a negative feedback loop in which the addition of new telomere repeats creates binding sites for inhibitors of telomere length extension. May also influence the balance of transcriptional silencing at telomeres and the silent mating type locus HMR, which is mediated by SIR (Silent Information Regulator) proteins including SIR3 and SIR4. RIF1 competes with SIR proteins for binding to the C-terminus of RAP1. In the absence of RIF1, a limiting cellular pool of SIR proteins may preferentially associate with RAP1 at sub-telomeric loci, causing enhanced telomeric silencing and attenuated silencing of the HMR locus.<ref>PMID:1577274</ref> <ref>PMID:7867933</ref> <ref>PMID:9087429</ref> <ref>PMID:10531008</ref> <ref>PMID:15572688</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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<ref>PMID:23746845</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4bjs" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Baker's yeast]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bunker, R D]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Gut, H]]
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[[Category: Bunker RD]]
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[[Category: Scrima, A]]
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[[Category: Gut H]]
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[[Category: Shi, T]]
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[[Category: Scrima A]]
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[[Category: Thoma, N H]]
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[[Category: Shi T]]
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[[Category: Cell cycle]]
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[[Category: Thoma NH]]
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[[Category: Telomere associated protein]]
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Current revision

Crystal structure of the Rif1 C-terminal domain (Rif1-CTD) from Saccharomyces cerevisiae

PDB ID 4bjs

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