<p>Meiotic telomeres play a critical role in chromosome dynamics, facilitating homolog pairing and synapsis through attachment to the nuclear envelope (NE). While these mechanisms are well-documented for standard A-set chromosomes, the molecular composition of supernumerary (or B) chromosome telomeres remains poorly understood. In this study, for the first time we investigated the distribution of key telomeric and NE-attachment proteins in Bs. Using immunocytochemistry and immuno-FISH on spermatocytes of the narrow-headed vole, <i>Lasiopodomys gregalis</i> (Rodentia, Mammalia), we identified the presence of the shelterin components RAP1, POT1 and TIN2; the LINC complex proteins SUN1 and KASH5; a major component of the nuclear lamina, Lamin B1; the regulatory kinase CDK2; and telomeric DNA specifically at the termini of meiotic supernumeraries. Our results demonstrate that despite their univalent nature and involvement in meiotic inactivation, Bs of this mammalian species possess a telomeric protein architecture that is highly similar, if even not identical, to that of A-set and sex chromosomes. These findings suggest that Bs are integrated into the meiotic machinery, utilizing standard protective and anchoring mechanisms to ensure genomic stability during prophase I.</p>

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Meiotic telomeres of vole B chromosomes: shelterin and associated proteins provide a link to the nuclear envelope

  • Sergey N. Matveevsky,
  • Tatyana V. Petrova,
  • Svetlana V. Pavlova

摘要

Meiotic telomeres play a critical role in chromosome dynamics, facilitating homolog pairing and synapsis through attachment to the nuclear envelope (NE). While these mechanisms are well-documented for standard A-set chromosomes, the molecular composition of supernumerary (or B) chromosome telomeres remains poorly understood. In this study, for the first time we investigated the distribution of key telomeric and NE-attachment proteins in Bs. Using immunocytochemistry and immuno-FISH on spermatocytes of the narrow-headed vole, Lasiopodomys gregalis (Rodentia, Mammalia), we identified the presence of the shelterin components RAP1, POT1 and TIN2; the LINC complex proteins SUN1 and KASH5; a major component of the nuclear lamina, Lamin B1; the regulatory kinase CDK2; and telomeric DNA specifically at the termini of meiotic supernumeraries. Our results demonstrate that despite their univalent nature and involvement in meiotic inactivation, Bs of this mammalian species possess a telomeric protein architecture that is highly similar, if even not identical, to that of A-set and sex chromosomes. These findings suggest that Bs are integrated into the meiotic machinery, utilizing standard protective and anchoring mechanisms to ensure genomic stability during prophase I.