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TitleStructures of nucleotide-bound human telomerase at several steps of its telomeric DNA repeat addition cycle.
Journal, issue, pagesNat Commun, Vol. 17, Issue 1, Page 1847, Year 2026
Publish dateJan 21, 2026
AuthorsSebastian Balch / Elsa Franco-Echevarría / George E Ghanim / Rachael C Kretsch / Rhiju Das / Thi Hoang Duong Nguyen /
PubMed AbstractIn most eukaryotes, the reverse transcriptase telomerase counteracts telomere shortening by processively adding telomeric DNA repeat sequences to chromosome ends. Telomerase activity depends on the ...In most eukaryotes, the reverse transcriptase telomerase counteracts telomere shortening by processively adding telomeric DNA repeat sequences to chromosome ends. Telomerase activity depends on the telomerase reverse transcriptase (TERT) and the telomerase RNA (hTR in humans). Processive telomere elongation is critical for genome stability, and defects in this mechanism are linked to cellular dysfunction and human disease. However, the structural basis for telomerase repeat addition processivity in humans has remained elusive. Here, we present cryo-electron microscopy structures of human telomerase bound to telomeric DNA and an incoming nucleotide, captured at three distinct stages of its repeat addition cycle: initiation, elongation, and pre-termination. Across these states, the TERT active site maintains a conserved architecture that stabilises a short DNA-RNA duplex of constant length of four base-pairs. Beyond the active site, we identify dynamic structural features in both TERT and hTR that facilitate substrate engagement and RNA template repositioning, thereby supporting the synthesis of successive telomeric repeats. Together, these structures provide key insights into how human telomerase achieves its unique processivity to maintain telomere length and genome integrity.
External linksNat Commun / PubMed:41565648 / PubMed Central
MethodsEM (single particle)
Resolution3.2 - 3.8 Å
Structure data

54920

9shy

EMDB-54920, PDB-9shy:
Cryo-EM structure of the catalytic core of human telomerase at the initiation state of the repeat addition cycle
Method: EM (single particle) / Resolution: 3.53 Å

54921

9shz

EMDB-54921, PDB-9shz:
Cryo-EM structure of the catalytic core of human telomerase at the elongation state of the repeat addition cycle
Method: EM (single particle) / Resolution: 3.2 Å

54922

9si0

EMDB-54922, PDB-9si0:
Cryo-EM structure of the catalytic core of human telomerase at the pre-termination state of the repeat addition cycle
Method: EM (single particle) / Resolution: 3.8 Å

Chemicals

ChemComp-1GC:
2'-deoxy-5'-O-[(R)-hydroxy{[(S)-hydroxy(phosphonooxy)phosphoryl]methyl}phosphoryl]guanosine

PDB-1acd:
V32D/F57H MUTANT OF MURINE ADIPOCYTE LIPID BINDING PROTEIN

Source
  • homo sapiens (human)
KeywordsRNA BINDING PROTEIN / telomerase / H/ACA

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