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Structural basis of meiotic telomere attachment to the nuclear envelope by MAJIN-TERB2-TERB1

Please always quote using this URN: urn:nbn:de:bvb:20-opus-226416
  • Meiotic chromosomes undergo rapid prophase movements, which are thought to facilitate the formation of inter-homologue recombination intermediates that underlie synapsis, crossing over and segregation. The meiotic telomere complex (MAJIN, TERB1, TERB2) tethers telomere ends to the nuclear envelope and transmits cytoskeletal forces via the LINC complex to drive these rapid movements. Here, we report the molecular architecture of the meiotic telomere complex through the crystal structure of MAJIN-TERB2, together with light and X-ray scatteringMeiotic chromosomes undergo rapid prophase movements, which are thought to facilitate the formation of inter-homologue recombination intermediates that underlie synapsis, crossing over and segregation. The meiotic telomere complex (MAJIN, TERB1, TERB2) tethers telomere ends to the nuclear envelope and transmits cytoskeletal forces via the LINC complex to drive these rapid movements. Here, we report the molecular architecture of the meiotic telomere complex through the crystal structure of MAJIN-TERB2, together with light and X-ray scattering studies of wider complexes. The MAJIN-TERB2 2:2 hetero-tetramer binds strongly to DNA and is tethered through long flexible linkers to the inner nuclear membrane and two TRF1-binding 1:1 TERB2-TERB1 complexes. Our complementary structured illumination microscopy studies and biochemical findings reveal a telomere attachment mechanism in which MAJIN-TERB2-TERB1 recruits telomere-bound TRF1, which is then displaced during pachytene, allowing MAJIN-TERB2-TERB1 to bind telomeric DNA and form a mature attachment plate.show moreshow less

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Metadaten
Author: James M. Dunce, Amy E. Milburn, Manickam Gurusaran, Irene da Cruz, Lee T. Sen, Ricardo Benavente, Owen R. Davies
URN:urn:nbn:de:bvb:20-opus-226416
Document Type:Journal article
Faculties:Fakultät für Biologie / Theodor-Boveri-Institut für Biowissenschaften
Language:English
Parent Title (English):Nature Communications
Year of Completion:2018
Volume:9
Article Number:5355
Source:Nature Communications (2018) 9:5355. https://doi.org/10.1038/s41467-018-07794-7
DOI:https://doi.org/10.1038/s41467-018-07794-7
Dewey Decimal Classification:5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie
Tag:DNA; X-ray crystallography; meiosis; proteins; super-resolution microscopy
Release Date:2024/06/14
Licence (German):License LogoCC BY: Creative-Commons-Lizenz: Namensnennung 4.0 International