Fig. 8
From: Structural basis of meiotic telomere attachment to the nuclear envelope by MAJIN-TERB2-TERB1
TRF1-mediated chromosomal attachment to the meiotic telomere complex. a–e Structured illumination microscopy. Wide-field images, plot analyses and additional orientations are shown in Supplementary Figs. 14 and 15. a Spread mouse zygotene spermatocyte chromosomes stained with anti-SYCP3 (green), anti-TRF1 (cyan) and anti-TERB1 (top) or anti-MAJIN (bottom) (magenta). Scale bars, 0.3 µm. b Structurally preserved mouse spermatocyte pachytene nuclei stained with anti-SYCP3 (green), anti-TRF1 (cyan) and anti-TERB1 (top) or anti-MAJIN (bottom) (magenta). Scale bars, 0.3 µm. c–e Spread mouse pachytene spermatocyte chromosomes stained with anti-SYCP3 (green) and (c) anti-TERB1 (magenta) and anti-TRF1 (cyan), (d) anti-MAJIN (magenta) and anti-TRF1 (cyan), and (e) anti-TERB2 (magenta) in combination with telomere fluorescence in situ hybridisation (cyan; TeloFISH). Scale bars, 0.3 µm and 0.5 µm. Normalised intensity-distance plots are shown; frontal plots represent averages of multiple images (n = 25 telomeres), other orientation plots represent individual images. Source data are provided as a Source Data file. f, g Model of meiotic telomere attachment to the nuclear envelope. f Telomere ends are initially recruited through TRF1, which interacts with the meiotic telomere complex via TERB1, mediating its indirect interaction with telomeres. g TRF1 is subsequently displaced, allowing the meiotic telomere complex to bind directly to telomeric DNA, with TRF1 associating with surrounding telomeric DNA.
