Fig. 1

Rapid prophase chromosomal movements through meiotic telomere-nuclear envelope tethering. a Meiotic chromosome telomere ends are tethered to the nuclear envelope by the meiotic telomere complex, enabling the transmission of cytoskeletal forces from microtubules to chromosome ends through LINC complexes. This produces rapid prophase chromosomal movements that are thought to facilitate recombination-mediated homology searches to generate inter-homologue recombination intermediates. The resulting pairings mature into synapsis through synaptonemal complex assembly, leading to crossover formation and the generation of single end attachment plates between synapsed telomere ends and the nuclear envelope. b Schematic of the domain structure and sequence conservation of human meiotic telomere complex proteins MAJIN, TERB1 and TERB2, and shelterin component TRF1. Amino acid conservation is illustrated as black plots in which the plot height represents the per residue conservation score. Sequences are annotated with their domain structure, interacting regions and oligomer states based on previous reports^42,43,44,45 and the results presented herein. MAJIN contains an N-terminal globular core (amino acids 1–112) that interacts with the TERB2 C-terminus (amino acids 168–220). The TERB2 N-terminus (amino acids 1–107) interacts with the TERB2-binding (T2B) site of TERB1 (amino acids 585–642), which is flanked by a wider TRF1-binding (TRFB) site (amino acids 561–658) that interacts with the TRF homology (TRFH) domain of TRF1 (amino acids 62–268). MAJIN contains a C-terminal transmembrane (TM) helix, whilst TERB1 and TRF1 both contain C-terminal DNA-binding MYB domains