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Dissecting the telomere-inner nuclear membrane interface formed in meiosis.

Journal article
Authors Devon F Pendlebury
Yasuhiro Fujiwara
Valerie M Tesmer
Eric M Smith
Hiroki Shibuya
Yoshinori Watanabe
Jayakrishnan Nandakumar
Published in Nature structural & molecular biology
Volume 24
Pages 1064–1072
ISSN 1545-9985
Publication year 2017
Published at Department of Chemistry and Molecular Biology
Pages 1064–1072
Language en
Subject categories Structural Biology, Cell Biology


Tethering telomeres to the inner nuclear membrane (INM) allows homologous chromosome pairing during meiosis. The meiosis-specific protein TERB1 binds the telomeric protein TRF1 to establish telomere-INM connectivity and is essential for mouse fertility. Here we solve the structure of the human TRF1-TERB1 interface to reveal the structural basis for telomere-INM linkage. Disruption of this interface abrogates binding and compromises telomere-INM attachment in mice. An embedded CDK-phosphorylation site within the TRF1-binding region of TERB1 provides a mechanism for cap exchange, a late-pachytene phenomenon involving the dissociation of the TRF1-TERB1 complex. Indeed, further strengthening this interaction interferes with cap exchange. Finally, our biochemical analysis implicates distinct complexes for telomere-INM tethering and chromosome-end protection during meiosis. Our studies unravel the structure, stoichiometry, and physiological implications underlying telomere-INM tethering, thereby providing unprecedented insights into the unique function of telomeres in meiosis.

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