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| ==Crystal structure of Ku70/80 and TLC1== | | ==Crystal structure of Ku70/80 and TLC1== |
| <StructureSection load='5y58' size='340' side='right' caption='[[5y58]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='5y58' size='340' side='right'caption='[[5y58]], [[Resolution|resolution]] 2.80Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[5y58]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [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=5Y58 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y58 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[5y58]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [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=5Y58 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Y58 FirstGlance]. <br> |
| </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YKU70, HDF1, NES24, YMR284W, YM8021.10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), YKU80, HDF2, YMR106C, YM9718.05C ([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]] 2.8Å</td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </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=5y58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y58 OCA], [https://pdbe.org/5y58 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5y58 RCSB], [https://www.ebi.ac.uk/pdbsum/5y58 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5y58 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=5y58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y58 OCA], [http://pdbe.org/5y58 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y58 RCSB], [http://www.ebi.ac.uk/pdbsum/5y58 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y58 ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/KU70_YEAST KU70_YEAST]] Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Appears to have a role in recruitment of telomerase and CDC13 to the telomere and the subsequent telomere elongation. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. KU70, of the KU70/KU80 heterodimer, binds to the stem loop of TLC1, the RNA component of telomerase. Involved in telomere maintenance. Interacts with telomeric repeats and subtelomeric sequences thereby controlling telomere length and protecting against subtelomeric rearrangement. Maintains telomeric chromatin, which is involved in silencing the expression of genes located at the telomere. Required for mating-type switching.<ref>PMID:10675560</ref> <ref>PMID:11046137</ref> <ref>PMID:12138180</ref> <ref>PMID:12975323</ref> <ref>PMID:14585978</ref> <ref>PMID:8626469</ref> <ref>PMID:8668537</ref> <ref>PMID:9635192</ref> <ref>PMID:9635193</ref> <ref>PMID:9663392</ref> <ref>PMID:9914366</ref> [[http://www.uniprot.org/uniprot/KU80_YEAST KU80_YEAST]] Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Appears to have a role in recruitment of telomerase and CDC13 to the telomere and the subsequent telomere elongation. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. KU70, of the KU70/KU80 heterodimer, binds to the stem loop of TLC1, the RNA component of telomerase. Involved in telomere maintenance. Interacts with telomeric repeats and subtelomeric sequences thereby controlling telomere length and protecting against subtelomeric rearrangement. Maintains telomeric chromatin, which is involved in silencing the expression of genes located at the telomere. Required for mating-type switching.<ref>PMID:10675560</ref> <ref>PMID:11046137</ref> <ref>PMID:12138180</ref> <ref>PMID:12975323</ref> <ref>PMID:14551211</ref> <ref>PMID:14585978</ref> <ref>PMID:16166630</ref> <ref>PMID:8910371</ref> <ref>PMID:8972848</ref> <ref>PMID:9563951</ref> <ref>PMID:9635192</ref> <ref>PMID:9635193</ref> <ref>PMID:9663392</ref> <ref>PMID:9914366</ref> | | [https://www.uniprot.org/uniprot/KU70_YEAST KU70_YEAST] Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Appears to have a role in recruitment of telomerase and CDC13 to the telomere and the subsequent telomere elongation. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. KU70, of the KU70/KU80 heterodimer, binds to the stem loop of TLC1, the RNA component of telomerase. Involved in telomere maintenance. Interacts with telomeric repeats and subtelomeric sequences thereby controlling telomere length and protecting against subtelomeric rearrangement. Maintains telomeric chromatin, which is involved in silencing the expression of genes located at the telomere. Required for mating-type switching.<ref>PMID:10675560</ref> <ref>PMID:11046137</ref> <ref>PMID:12138180</ref> <ref>PMID:12975323</ref> <ref>PMID:14585978</ref> <ref>PMID:8626469</ref> <ref>PMID:8668537</ref> <ref>PMID:9635192</ref> <ref>PMID:9635193</ref> <ref>PMID:9663392</ref> <ref>PMID:9914366</ref> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Telomerase maintains chromosome ends from humans to yeasts. Recruitment of yeast telomerase to telomeres occurs through its Ku and Est1 subunits via independent interactions with telomerase RNA (TLC1) and telomeric proteins Sir4 and Cdc13, respectively. However, the structures of the molecules comprising these telomerase-recruiting pathways remain unknown. Here, we report crystal structures of the Ku heterodimer and Est1 complexed with their key binding partners. Two major findings are as follows: (1) Ku specifically binds to telomerase RNA in a distinct, yet related, manner to how it binds DNA; and (2) Est1 employs two separate pockets to bind distinct motifs of Cdc13. The N-terminal Cdc13-binding site of Est1 cooperates with the TLC1-Ku-Sir4 pathway for telomerase recruitment, whereas the C-terminal interface is dispensable for binding Est1 in vitro yet is nevertheless essential for telomere maintenance in vivo. Overall, our results integrate previous models and provide fundamentally valuable structural information regarding telomere biology.
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| Structural Insights into Yeast Telomerase Recruitment to Telomeres.,Chen H, Xue J, Churikov D, Hass EP, Shi S, Lemon LD, Luciano P, Bertuch AA, Zappulla DC, Geli V, Wu J, Lei M Cell. 2018 Jan 11;172(1-2):331-343.e13. doi: 10.1016/j.cell.2017.12.008. Epub, 2017 Dec 28. PMID:29290466<ref>PMID:29290466</ref>
| | ==See Also== |
| | | *[[Helicase 3D structures|Helicase 3D structures]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| | *[[Ku protein|Ku protein]] |
| </div>
| |
| <div class="pdbe-citations 5y58" style="background-color:#fffaf0;"></div>
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| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Baker's yeast]] | | [[Category: Large Structures]] |
| [[Category: DNA helicase]] | | [[Category: Saccharomyces cerevisiae]] |
| [[Category: Chen, H]] | | [[Category: Saccharomyces cerevisiae S288C]] |
| [[Category: Lei, M]] | | [[Category: Chen H]] |
| [[Category: Wu, J]] | | [[Category: Lei M]] |
| [[Category: Xue, J]] | | [[Category: Wu J]] |
| [[Category: Protein-rna complex]]
| | [[Category: Xue J]] |
| [[Category: Rna binding protein]]
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| [[Category: Telomerase]]
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| [[Category: Telomere]]
| |