5we2: Difference between revisions

Latest revision as of 07:42, 17 October 2024

Structural Basis for Telomere Length Regulation by the Shelterin Bridge

Structural highlights

5we2 is a 5 chain structure with sequence from Schizosaccharomyces pombe 972h-. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.5Å
Ligands:	ZN
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

POZ1_SCHPO Telomeric DNA-binding protein that negatively regulates telomerase and telomere length.^[1]

Publication Abstract from PubMed

Telomere elongation through telomerase enables chromosome survival during cellular proliferation. The conserved multifunctional shelterin complex associates with telomeres to coordinate multiple telomere activities, including telomere elongation by telomerase. Similar to the human shelterin, fission yeast shelterin is composed of telomeric sequence-specific double- and single-stranded DNA-binding proteins, Taz1 and Pot1, respectively, bridged by Rap1, Poz1, and Tpz1. Here, we report the crystal structure of the fission yeast Tpz1(475-508)-Poz1-Rap1(467-496) complex that provides the structural basis for shelterin bridge assembly. Biochemical analyses reveal that shelterin bridge assembly is a hierarchical process in which Tpz1 binding to Poz1 elicits structural changes in Poz1, allosterically promoting Rap1 binding to Poz1. Perturbation of the cooperative Tpz1-Poz1-Rap1 assembly through mutation of the "conformational trigger" in Poz1 leads to unregulated telomere lengthening. Furthermore, we find that the human shelterin counterparts TPP1-TIN2-TRF2 also assemble hierarchically, indicating cooperativity as a conserved driving force for shelterin assembly.

Structural Basis for Shelterin Bridge Assembly.,Kim JK, Liu J, Hu X, Yu C, Roskamp K, Sankaran B, Huang L, Komives EA, Qiao F Mol Cell. 2017 Nov 16;68(4):698-714.e5. doi: 10.1016/j.molcel.2017.10.032. PMID:29149597^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Miyoshi T, Kanoh J, Saito M, Ishikawa F. Fission yeast Pot1-Tpp1 protects telomeres and regulates telomere length. Science. 2008 Jun 6;320(5881):1341-4. doi: 10.1126/science.1154819. PMID:18535244 doi:https://dx.doi.org/10.1126/science.1154819
↑ Kim JK, Liu J, Hu X, Yu C, Roskamp K, Sankaran B, Huang L, Komives EA, Qiao F. Structural Basis for Shelterin Bridge Assembly. Mol Cell. 2017 Nov 16;68(4):698-714.e5. doi: 10.1016/j.molcel.2017.10.032. PMID:29149597 doi:https://dx.doi.org/10.1016/j.molcel.2017.10.032

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OCA

[1] Miyoshi T, Kanoh J, Saito M, Ishikawa F. Fission yeast Pot1-Tpp1 protects telomeres and regulates telomere length. Science. 2008 Jun 6;320(5881):1341-4. doi: 10.1126/science.1154819. PMID:18535244 doi:https://dx.doi.org/10.1126/science.1154819

[2] Kim JK, Liu J, Hu X, Yu C, Roskamp K, Sankaran B, Huang L, Komives EA, Qiao F. Structural Basis for Shelterin Bridge Assembly. Mol Cell. 2017 Nov 16;68(4):698-714.e5. doi: 10.1016/j.molcel.2017.10.032. PMID:29149597 doi:https://dx.doi.org/10.1016/j.molcel.2017.10.032

[1]

[2]

@@ Line 1: / Line 1: @@
 ==Structural Basis for Telomere Length Regulation by the Shelterin Bridge==
-<StructureSection load='5we2' size='340' side='right' caption='[[5we2]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+<StructureSection load='5we2' size='340' side='right'caption='[[5we2]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5we2]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WE2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WE2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5we2]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WE2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WE2 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.5&#8491;</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=5we2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5we2 OCA], [http://pdbe.org/5we2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5we2 RCSB], [http://www.ebi.ac.uk/pdbsum/5we2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5we2 ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5we2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5we2 OCA], [https://pdbe.org/5we2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5we2 RCSB], [https://www.ebi.ac.uk/pdbsum/5we2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5we2 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/POZ1_SCHPO POZ1_SCHPO]] Telomeric DNA-binding protein that negatively regulates telomerase and telomere length.<ref>PMID:18535244</ref>  [[http://www.uniprot.org/uniprot/RAP1_SCHPO RAP1_SCHPO]] Involved in the regulation of telomere length, clustering and has a specific role in telomere position effect (TPE). Unlike yeast, exhibits no effect in transcription regulation.<ref>PMID:11676924</ref> <ref>PMID:11676925</ref> <ref>PMID:19948484</ref>  [[http://www.uniprot.org/uniprot/TPZ1_SCHPO TPZ1_SCHPO]] Telomeric DNA-binding protein that is required to protect the 3'-end telomeric overhang and involved in telomere length regulation. recruits poz1 and ccq1 to telomeres, regulating telomere length negatively and positivels respectively.<ref>PMID:16303567</ref> <ref>PMID:18535244</ref>
+[https://www.uniprot.org/uniprot/POZ1_SCHPO POZ1_SCHPO] Telomeric DNA-binding protein that negatively regulates telomerase and telomere length.<ref>PMID:18535244</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Hu, X]]
+[[Category: Large Structures]]
-[[Category: Kim, J K]]
+[[Category: Schizosaccharomyces pombe 972h-]]
-[[Category: Liu, J]]
+[[Category: Hu X]]
-[[Category: Qiao, F]]
+[[Category: Kim J-K]]
-[[Category: Sankaran, B]]
+[[Category: Liu J]]
-[[Category: Cooperativity]]
+[[Category: Qiao F]]
-[[Category: Gene regulation]]
+[[Category: Sankaran B]]
-[[Category: Shelterin]]
-[[Category: Telomere]]

5we2: Difference between revisions

Latest revision as of 07:42, 17 October 2024

Structural Basis for Telomere Length Regulation by the Shelterin Bridge

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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