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TitleThe architecture of Tetrahymena telomerase holoenzyme.
Journal, issue, pagesNature, Vol. 496, Issue 7444, Page 187-192, Year 2013
Publish dateApr 11, 2013
AuthorsJiansen Jiang / Edward J Miracco / Kyungah Hong / Barbara Eckert / Henry Chan / Darian D Cash / Bosun Min / Z Hong Zhou / Kathleen Collins / Juli Feigon /
PubMed AbstractTelomerase adds telomeric repeats to chromosome ends using an internal RNA template and a specialized telomerase reverse transcriptase (TERT), thereby maintaining genome integrity. Little is known ...Telomerase adds telomeric repeats to chromosome ends using an internal RNA template and a specialized telomerase reverse transcriptase (TERT), thereby maintaining genome integrity. Little is known about the physical relationships among protein and RNA subunits within a biologically functional holoenzyme. Here we describe the architecture of Tetrahymena thermophila telomerase holoenzyme determined by electron microscopy. Six of the seven proteins and the TERT-binding regions of telomerase RNA (TER) have been localized by affinity labelling. Fitting with high-resolution structures reveals the organization of TERT, TER and p65 in the ribonucleoprotein (RNP) catalytic core. p50 has an unanticipated role as a hub between the RNP catalytic core, p75-p19-p45 subcomplex, and the DNA-binding Teb1. A complete in vitro holoenzyme reconstitution assigns function to these interactions in processive telomeric repeat synthesis. These studies provide the first view of the extensive network of subunit associations necessary for telomerase holoenzyme assembly and physiological function.
External linksNature / PubMed:23552895 / PubMed Central
MethodsEM (single particle)
Resolution25.0 - 35.0 Å
Structure data

EMDB-5804:
Three-dimensional structure of endogenously assembled Tetrahymena telomerase holoenzyme determined by negative-stain electron microscopy
Method: EM (single particle) / Resolution: 25.0 Å

EMDB-5807:
Negative-stain electron microscopy reconstruction of Tetrahymena telomerase (Teb1-f, conformation II)
Method: EM (single particle) / Resolution: 30.0 Å

EMDB-5808:
Negative-stain electron microscopy reconstruction of Tetrahymena telomerase (Teb1-f, conformation III)
Method: EM (single particle) / Resolution: 30.0 Å

EMDB-5809:
Negative-stain electron microscopy reconstruction of Tetrahymena telomerase (Teb1-f, conformation IV)
Method: EM (single particle) / Resolution: 30.0 Å

EMDB-5810:
Negative-stain electron microscopy reconstruction of Tetrahymena telomerase (Teb1-f, conformation V)
Method: EM (single particle) / Resolution: 30.0 Å

EMDB-5811:
Negative-stain electron microscopy reconstruction of Tetrahymena telomerase (Teb1-f, conformation VI)
Method: EM (single particle) / Resolution: 30.0 Å

EMDB-5812:
Negative-stain electron microscopy reconstruction of Tetrahymena telomerase (Teb1-f, conformation VII)
Method: EM (single particle) / Resolution: 30.0 Å

EMDB-5813:
Negative-stain electron microscopy reconstruction of Tetrahymena telomerase (Teb1-f, conformation VIII)
Method: EM (single particle) / Resolution: 30.0 Å

EMDB-5814:
Negative-stain electron microscopy reconstruction of Tetrahymena telomerase (Teb1-f, conformation IX)
Method: EM (single particle) / Resolution: 30.0 Å

EMDB-5815:
Negative-stain electron microscopy reconstruction of Tetrahymena telomerase (Teb1-f, conformation X)
Method: EM (single particle) / Resolution: 30.0 Å

EMDB-5816:
Negative-stain electron microscopy reconstruction of Tetrahymena telomerase (TERT-f, stable conformation)
Method: EM (single particle) / Resolution: 35.0 Å

EMDB-5817:
Negative-stain electron microscopy reconstruction of Tetrahymena telomerase (TERT-f, subcomplex lacking p65 N-terminus)
Method: EM (single particle) / Resolution: 35.0 Å

EMDB-5818:
Negative-stain electron microscopy reconstruction of Tetrahymena telomerase (TERT-f, subcomplex lacking Teb1)
Method: EM (single particle) / Resolution: 35.0 Å

EMDB-5819:
Negative-stain electron microscopy reconstruction of Tetrahymena telomerase (TERT-f, subcomplex lacking p75-p19-p45)
Method: EM (single particle) / Resolution: 35.0 Å

EMDB-5820:
Negative-stain electron microscopy reconstruction of Tetrahymena telomerase (f-Teb1C, stable conformation)
Method: EM (single particle) / Resolution: 30.0 Å

EMDB-5821:
Negative-stain electron microscopy reconstruction of Tetrahymena telomerase (TERT-f, affinity labeled by anti-FLAG Fab)
Method: EM (single particle) / Resolution: 30.0 Å

EMDB-5822:
Negative-stain electron microscopy reconstruction of Tetrahymena telomerase (Teb1-f, affinity labeled by anti-FLAG Fab)
Method: EM (single particle) / Resolution: 30.0 Å

EMDB-5823:
Negative-stain electron microscopy reconstruction of Tetrahymena telomerase (f-p50, affinity labeled by two copies of anti-FLAG Fab)
Method: EM (single particle) / Resolution: 30.0 Å

EMDB-5824:
Negative-stain electron microscopy reconstruction of Tetrahymena telomerase (f-p50, affinity labeled by one copy of anti-FLAG Fab)
Method: EM (single particle) / Resolution: 30.0 Å

Source
  • Tetrahymena thermophila (eukaryote)
  • Mus musculus (house mouse)

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