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

Lookup NU author(s): James Dunce, Amy Milburn, Lee Sen, Dr Owen Davies

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This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).

Abstract

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 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.

Publication metadata

Author(s): Dunce JM, Milburn AE, Gurusaran M, Cruz Id, Sen LT, Benavente R, Davies OR

Publication type: Article

Publication status: Published

Journal: Nature Communications

Year: 2018

Volume: 9

Print publication date: 17/12/2018

Online publication date: 17/12/2018

Acceptance date: 27/11/2018

Date deposited: 17/12/2018

ISSN (electronic): 2041-1723

Publisher: Nature Publishing Group

URL: https://doi.org/10.1038/s41467-018-07794-7

DOI: 10.1038/s41467-018-07794-7

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