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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
Links dx.doi.org/10.1038/nsmb.3493
www.ncbi.nlm.nih.gov/entrez/query.f...
Subject categories Structural Biology, Cell Biology

Abstract

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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