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TitleCryo-electron microscopy structure of the budding yeast telomerase holoenzyme.
Journal, issue, pagesScience, Vol. 391, Issue 6792, Page eadz5344, Year 2026
Publish dateMar 26, 2026
AuthorsHongmiao Hu / Hannah Neumann / Gabriela M Teplitz / Elsa Franco-Echevarría / Pascal Chartrand / Raymund J Wellinger / Thi Hoang Duong Nguyen /
PubMed AbstractTelomerase is a reverse transcriptase that synthesizes telomeric repeats at chromosome ends, safeguarding genome integrity. We present the cryo-electron microscopy structure of the budding yeast ...Telomerase is a reverse transcriptase that synthesizes telomeric repeats at chromosome ends, safeguarding genome integrity. We present the cryo-electron microscopy structure of the budding yeast telomerase, which exhibits substantial divergence from its ciliate and vertebrate counterparts. The structure reveals a stable core formed by telomerase RNA TLC1; the three ever shorter telomere (Est) proteins, Est1, Est2 and Est3; and the Pop1/Pop6/Pop7 complex (Pop1/6/7). TLC1, Est3, and Pop1/6/7 serve critical roles in complex assembly. We identified a zinc finger (ZnF) motif in the telomerase reverse transcriptase (TERT) subunit Est2 that is crucial for telomerase function. Structure prediction suggests the presence of ZnFs in TERT from diverse species. These findings offer insights into the functional organization of yeast telomerase and underscore the evolutionary diversity of telomerase holoenzymes.
External linksScience / PubMed:41886584
MethodsEM (single particle)
Resolution3.0 - 3.7 Å
Structure data

EMDB-55321, PDB-9swn:
Cryo-EM structure of yeast telomerase holoenzyme
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-55322, PDB-9swo:
The catalytic core of yeast telomerase holoenzyme
Method: EM (single particle) / Resolution: 3.7 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

Source
  • Homo sapiens (human)
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsRNA BINDING PROTEIN / Telomerase / Telomerase RNA

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