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The TRF1-binding protein TERB1 promotes chromosome movement and telomere rigidity in meiosis
The TRF1-binding protein TERB1 promotes chromosome movement and telomere rigidity in meiosis
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The TRF1-binding protein TERB1 promotes chromosome movement and telomere rigidity in meiosis
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The TRF1-binding protein TERB1 promotes chromosome movement and telomere rigidity in meiosis
The TRF1-binding protein TERB1 promotes chromosome movement and telomere rigidity in meiosis

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The TRF1-binding protein TERB1 promotes chromosome movement and telomere rigidity in meiosis
The TRF1-binding protein TERB1 promotes chromosome movement and telomere rigidity in meiosis
Journal Article

The TRF1-binding protein TERB1 promotes chromosome movement and telomere rigidity in meiosis

2014
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Overview
During meiotic prophase, telomere-mediated chromosomal movement along the nuclear envelope is crucial for homologue pairing and synapsis. However, how telomeres are modified to mediate chromosome movement is largely elusive. Here we show that mammalian meiotic telomeres are fundamentally modified by a meiosis-specific Myb-domain protein, TERB1, that localizes at telomeres in mouse germ cells. TERB1 forms a heterocomplex with the canonical telomeric protein TRF1 and binds telomere repeat DNA. Disruption of Terb1 in mice abolishes meiotic chromosomal movement and impairs homologous pairing and synapsis, causing infertility in both sexes. TERB1 promotes telomere association with the nuclear envelope and deposition of the SUN–KASH complex, which recruits cytoplasmic motor complexes. TERB1 also binds and recruits cohesin to telomeres to develop structural rigidity, strikingly reminiscent of centromeres. Our study suggests that TERB1 acts as a central hub for the assembly of a conserved meiotic telomere complex required for chromosome movements. Meiotic chromosome movement is needed for homologue pairing and synapsis. Watanabe and colleagues identify TERB1 as a protein needed for telomere mobility and attachment to the nuclear envelope, and for telomere enrichment of meiotic cohesin.