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

DOI: 10.1038/s41467-018-07794-7 DOI Help

Authors: James M. Dunce (Newcastle University) , Amy E. Milburn (Newcastle University) , Manickam Gurusaran (Newcastle University) , Irene Da Cruz (University of Würzburg) , Lee T. Sen (Newcastle University) , Ricardo Benavente (University of Würzburg) , Owen R. Davies (Newcastle University)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 9

State: Published (Approved)
Published: December 2018
Diamond Proposal Number(s): 13587 , 15836 , 18598

Open Access Open Access

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.

Journal Keywords: DNA; Meiosis; Proteins; Super-resolution microscopy; X-ray crystallography

Subject Areas: Biology and Bio-materials


Instruments: B21-High Throughput SAXS , I03-Macromolecular Crystallography , I04-1-Macromolecular Crystallography (fixed wavelength) , I04-Macromolecular Crystallography

Documents:
s41467-018-07794-7.pdf