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| | ==Structure of the TRF1-TERB1 interface== | | ==Structure of the TRF1-TERB1 interface== |
| - | <StructureSection load='5wir' size='340' side='right' caption='[[5wir]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='5wir' size='340' side='right'caption='[[5wir]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5wir]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WIR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WIR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5wir]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WIR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WIR FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TERF1, PIN2, TRBF1, TRF, TRF1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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]] 2.1Å</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=5wir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wir OCA], [http://pdbe.org/5wir PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wir RCSB], [http://www.ebi.ac.uk/pdbsum/5wir PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wir 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=5wir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wir OCA], [https://pdbe.org/5wir PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wir RCSB], [https://www.ebi.ac.uk/pdbsum/5wir PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wir ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TERF1_HUMAN TERF1_HUMAN]] Binds the telomeric double-stranded TTAGGG repeat and negatively regulates telomere length. Involved in the regulation of the mitotic spindle. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways.<ref>PMID:16166375</ref> | + | [https://www.uniprot.org/uniprot/TERB1_HUMAN TERB1_HUMAN] Meiosis-specific telomere-associated protein involved in meiotic telomere attachment to the nucleus inner membrane, a crucial step for homologous pairing and synapsis. Component of the MAJIN-TERB1-TERB2 complex, which promotes telomere cap exchange by mediating attachment of telomeric DNA to the inner nuclear membrane and replacement of the protective cap of telomeric chromosomes: in early meiosis, the MAJIN-TERB1-TERB2 complex associates with telomeric DNA and the shelterin/telosome complex. During prophase, the complex matures and promotes release of the shelterin/telosome complex from telomeric DNA. In the MAJIN-TERB1-TERB2 complex, TERB1 probably mediates association with the shelterin/telosome complex via interaction with TERF1, promoting priming telomeric DNA attachment'. Promotes telomere association with the nuclear envelope and deposition of the SUN-KASH/LINC complex. Also recruits cohesin to telomeres to develop structural rigidity.[UniProtKB:Q8C0V1] |
| | <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: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Nandakumar, J]] | + | [[Category: Large Structures]] |
| - | [[Category: Pendlebury, D F]] | + | [[Category: Nandakumar J]] |
| - | [[Category: Smith, E M]] | + | [[Category: Pendlebury DF]] |
| - | [[Category: Tesmer, V M]] | + | [[Category: Smith EM]] |
| - | [[Category: Cdk phosphorylation]] | + | [[Category: Tesmer VM]] |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Meiosis]]
| + | |
| - | [[Category: Telomere]]
| + | |
| Structural highlights
Function
TERB1_HUMAN Meiosis-specific telomere-associated protein involved in meiotic telomere attachment to the nucleus inner membrane, a crucial step for homologous pairing and synapsis. Component of the MAJIN-TERB1-TERB2 complex, which promotes telomere cap exchange by mediating attachment of telomeric DNA to the inner nuclear membrane and replacement of the protective cap of telomeric chromosomes: in early meiosis, the MAJIN-TERB1-TERB2 complex associates with telomeric DNA and the shelterin/telosome complex. During prophase, the complex matures and promotes release of the shelterin/telosome complex from telomeric DNA. In the MAJIN-TERB1-TERB2 complex, TERB1 probably mediates association with the shelterin/telosome complex via interaction with TERF1, promoting priming telomeric DNA attachment'. Promotes telomere association with the nuclear envelope and deposition of the SUN-KASH/LINC complex. Also recruits cohesin to telomeres to develop structural rigidity.[UniProtKB:Q8C0V1]
Publication Abstract from PubMed
Tethering telomeres to the inner nuclear membrane (INM) allows homologous chromosome pairing during meiosis. The meiosis-specific protein TERB1 binds the telomeric protein TRF1 to establish telomere-INM connectivity and is essential for mouse fertility. Here we solve the structure of the human TRF1-TERB1 interface to reveal the structural basis for telomere-INM linkage. Disruption of this interface abrogates binding and compromises telomere-INM attachment in mice. An embedded CDK-phosphorylation site within the TRF1-binding region of TERB1 provides a mechanism for cap exchange, a late-pachytene phenomenon involving the dissociation of the TRF1-TERB1 complex. Indeed, further strengthening this interaction interferes with cap exchange. Finally, our biochemical analysis implicates distinct complexes for telomere-INM tethering and chromosome-end protection during meiosis. Our studies unravel the structure, stoichiometry, and physiological implications underlying telomere-INM tethering, thereby providing unprecedented insights into the unique function of telomeres in meiosis.
Dissecting the telomere-inner nuclear membrane interface formed in meiosis.,Pendlebury DF, Fujiwara Y, Tesmer VM, Smith EM, Shibuya H, Watanabe Y, Nandakumar J Nat Struct Mol Biol. 2017 Oct 30. doi: 10.1038/nsmb.3493. PMID:29083414[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pendlebury DF, Fujiwara Y, Tesmer VM, Smith EM, Shibuya H, Watanabe Y, Nandakumar J. Dissecting the telomere-inner nuclear membrane interface formed in meiosis. Nat Struct Mol Biol. 2017 Oct 30. doi: 10.1038/nsmb.3493. PMID:29083414 doi:http://dx.doi.org/10.1038/nsmb.3493
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