5WIR

Structure of the TRF1-TERB1 interface

5WIR の概要

• エントリーDOI: 10.2210/pdb5wir/pdb
• 分子名称: TERB1-TBM, Telomeric repeat-binding factor 1 (3 entities in total)
• 機能のキーワード: meiosis, telomere, cdk phosphorylation, dna binding protein
• 由来する生物種: Homo sapiens; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 50544.24

構造登録者

Nandakumar, J.,Pendlebury, D.F.,Smith, E.M.,Tesmer, V.M. (登録日: 2017-07-20, 公開日: 2017-10-18, 最終更新日: 2023-10-04)

主引用文献

Pendlebury, D.F.,Fujiwara, Y.,Tesmer, V.M.,Smith, E.M.,Shibuya, H.,Watanabe, Y.,Nandakumar, J.
Dissecting the telomere-inner nuclear membrane interface formed in meiosis.
Nat. Struct. Mol. Biol., 24:1064-1072, 2017

PubMed 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.

PubMed: 29083414
DOI: 10.1038/nsmb.3493

実験手法

X-RAY DIFFRACTION (2.1 Å)