9QB2

H/ACA RNP protomer of human telomerase dimer

これはPDB形式変換不可エントリーです。

9QB2 の概要

• エントリーDOI: 10.2210/pdb9qb2/pdb
• EMDBエントリー: 52983
• 分子名称: H/ACA ribonucleoprotein complex subunit DKC1, H/ACA ribonucleoprotein complex subunit 1, H/ACA ribonucleoprotein complex subunit 2, ... (6 entities in total)
• 機能のキーワード: telomerase, h/aca, rna-binding protein, rna binding protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 11
• 化学式量合計: 560539.13

構造登録者

Balch, S.,Sekne, Z.,Franco-Echevarria, E.,Ludzia, P.,Kretsch, R.C.,Sun, W.,Yu, H.,Ghanim, G.E.,Sigurdur, T.R.,Ding, Y.,Das, R.,Nguyen, T.H.D. (登録日: 2025-02-28, 公開日: 2025-07-16, 最終更新日: 2025-07-23)

主引用文献

Balch, S.,Sekne, Z.,Franco-Echevarria, E.,Ludzia, P.,Kretsch, R.C.,Sun, W.,Yu, H.,Ghanim, G.E.,Thorkelsson, S.,Ding, Y.,Das, R.,Nguyen, T.H.D.
Cryo-EM structure of human telomerase dimer reveals H/ACA RNP-mediated dimerization.
Science, 389:eadr5817-eadr5817, 2025

PubMed Abstract: Telomerase ribonucleoprotein (RNP) synthesizes telomeric repeats at chromosome ends using a telomerase reverse transcriptase (TERT) and a telomerase RNA (hTR in humans). Previous structural work showed that human telomerase is typically monomeric, containing a single copy of TERT and hTR. Evidence for dimeric complexes exists, although the composition, high-resolution structure, and function remain elusive. Here, we report the cryo-electron microscopy (cryo-EM) structure of a human telomerase dimer bound to telomeric DNA. The structure reveals a 26-subunit assembly and a dimerization interface mediated by the Hinge and ACA box (H/ACA) RNP of telomerase. Premature aging disease mutations map to this interface. Disrupting dimer formation affects RNP assembly, bulk telomerase activity, and telomere maintenance in cells. Our findings address a long-standing enigma surrounding the telomerase dimer and suggest a role for the dimer in telomerase assembly.

PubMed: 40638752
DOI: 10.1126/science.adr5817

実験手法

ELECTRON MICROSCOPY (3 Å)