Transmembrane protein Sun2 is involved in tethering mammalian meiotic telomeres to the nuclear envelope

Johannes Schmitt, Ricardo Benavente, Didier Hodzic, Christer Höög, Colin L. Stewart, Manfred Alsheimer

Research output: Contribution to journalArticlepeer-review

133 Scopus citations

Abstract

Dynamic repositioning of telomeres is a unique feature of meiotic prophase I that is highly conserved among eukaryotes. At least in fission yeast it was shown to be required for proper alignment and recombination of homologous chromosomes. On entry into meiosis telomeres attach to the nuclear envelope and transiently cluster at a limited area to form a chromosomal bouquet. Telomere clustering is thought to promote chromosome recognition and stable pairing of the homologs. However, the molecular basis of telomere attachment and movement is largely unknown. Here we report that mammalian SUN-domain protein Sun2 specifically localizes to the nuclear envelope attachment sites of meiotic telomeres. Sun2-telomere association is maintained throughout the dynamic movement of telomeres. This association does not require the assembly of chromosomal axial elements or the presence of A-type lamins. Detailed EM analysis revealed that Sun2 is part of a membrane-spanning fibrillar complex that interconnects attached telomeres with cytoplasmic structures. Together with recent findings in fission yeast, our study indicates that the molecular mechanisms required for tethering meiotic telomeres and their dynamic movements during bouquet formation are conserved among eukaryotes.

Original languageEnglish
Pages (from-to)7426-7431
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume104
Issue number18
DOIs
StatePublished - May 1 2007

Keywords

  • Meiosis
  • SUN-domain proteins
  • Telomere attachment

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