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Cryo-EM structure of human telomerase dimer reveals H/ACA RNP-mediated dimerization.

Sebastian Balch1, Zala Sekne1, Elsa Franco-Echevarría1

  • 1MRC Laboratory of Molecular Biology, Cambridge, UK.

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|July 10, 2025
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Summary
This summary is machine-generated.

This study reveals the cryo-EM structure of a human telomerase dimer, a 26-subunit complex. This dimer formation, mediated by the Hinge and ACA box (H/ACA) RNP, is crucial for telomerase assembly and function.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Human telomerase is a ribonucleoprotein (RNP) complex responsible for synthesizing telomeric repeats.
  • Telomerase typically exists as a monomer, but dimeric forms have been observed, with their structure and function poorly understood.

Purpose of the Study:

  • To determine the high-resolution structure of the human telomerase dimer.
  • To elucidate the composition and functional implications of telomerase dimerization.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was used to determine the structure of the human telomerase dimer bound to telomeric DNA.
  • Analysis of premature aging disease mutations in relation to the dimerization interface.

Main Results:

  • The cryo-EM structure reveals a 26-subunit human telomerase dimer.
  • A dimerization interface mediated by the Hinge and ACA box (H/ACA) RNP was identified.
  • Premature aging disease mutations were found to map to this dimerization interface.

Conclusions:

  • The study provides the first high-resolution structure of a human telomerase dimer.
  • Dimer formation is critical for telomerase ribonucleoprotein (RNP) assembly, telomerase activity, and telomere maintenance.
  • The findings suggest a significant role for the telomerase dimer in the overall assembly and function of the enzyme.