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| | <StructureSection load='4bj6' size='340' side='right'caption='[[4bj6]], [[Resolution|resolution]] 3.26Å' scene=''> | | <StructureSection load='4bj6' size='340' side='right'caption='[[4bj6]], [[Resolution|resolution]] 3.26Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4bj6]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BJ6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BJ6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4bj6]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BJ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BJ6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 3.26Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4bj1|4bj1]], [[4bj5|4bj5]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4bj6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bj6 OCA], [http://pdbe.org/4bj6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bj6 RCSB], [http://www.ebi.ac.uk/pdbsum/4bj6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bj6 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=4bj6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bj6 OCA], [https://pdbe.org/4bj6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bj6 RCSB], [https://www.ebi.ac.uk/pdbsum/4bj6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bj6 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. [[http://www.uniprot.org/uniprot/RAP1_YEAST RAP1_YEAST]] Essential regulatory protein in yeast whose DNA-binding sites are found at three types of chromosomal elements: promoters, silencers, and telomeres. RAP1 is also involved in the regulation of telomere structure, where its binding sites are found within the terminal poly[C(1-3)A] sequences. The opposite regulatory functions of RAP1 are not intrinsic to its binding sites but, instead, result from interactions with different factors at promoters and silencers. RAP1 associates with SIR3 and SIR4 proteins to form a DNA-binding complex that initiates the repression at the HM loci and telomeres. May also target the binding of RIF1 and RIF2 to silencers and telomeres. Forms with GCR1 a transcriptional activation complex that is required for expression of glycolytic and ribosomal gene. | + | [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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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bunker, R D]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[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: Genome stability]]
| + | |
| - | [[Category: Telomere associated protein]]
| + | |
| - | [[Category: Transcription]]
| + | |
| 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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