telomerase catalytic core complex assembly / telomerase RNA stabilization / telomerase catalytic core complex / : / DNA replication factor A complex / single-stranded telomeric DNA binding / telomerase holoenzyme complex / telomerase RNA binding / telomeric DNA binding / telomere maintenance via telomerase ...telomerase catalytic core complex assembly / telomerase RNA stabilization / telomerase catalytic core complex / : / DNA replication factor A complex / single-stranded telomeric DNA binding / telomerase holoenzyme complex / telomerase RNA binding / telomeric DNA binding / telomere maintenance via telomerase / RNA-directed DNA polymerase / chromosome, telomeric region / DNA replication / DNA recombination / DNA repair / DNA binding / zinc ion binding / metal ion binding Similarity search - Function
: / Telomerase reverse transcriptase TEN domain / Replication factor A protein 3 / Replication factor A protein 3 / xRRM domain profile. / La protein, xRRM domain / La domain containing protein / La domain / Domain in the RNA-binding Lupus La protein; unknown function / La-type HTH domain ...: / Telomerase reverse transcriptase TEN domain / Replication factor A protein 3 / Replication factor A protein 3 / xRRM domain profile. / La protein, xRRM domain / La domain containing protein / La domain / Domain in the RNA-binding Lupus La protein; unknown function / La-type HTH domain / La-type HTH domain profile. / Telomerase ribonucleoprotein complex - RNA binding domain / : / Telomerase reverse transcriptase / Telomerase ribonucleoprotein complex - RNA-binding domain / Telomerase ribonucleoprotein complex - RNA binding domain / Replication factor A, C-terminal / Replication factor-A C terminal domain / RNA recognition motif / RNA recognition motif / Eukaryotic RNA Recognition Motif (RRM) profile. / RNA recognition motif domain / RNA-binding domain superfamily / Reverse transcriptase (RNA-dependent DNA polymerase) / Reverse transcriptase domain / Reverse transcriptase (RT) catalytic domain profile. / Winged helix DNA-binding domain superfamily / Nucleotide-binding alpha-beta plait domain superfamily / Winged helix-like DNA-binding domain superfamily / Nucleic acid-binding, OB-fold Similarity search - Domain/homology
Replication protein A 32 kDa subunit / Replication protein A 14 kDa subunit / Telomerase-associated protein of 75 kDa / Telomeric repeat-binding subunit 1 / Telomerase-associated protein of 19 kDa / Telomerase-associated protein of 50 kDa / Telomerase reverse transcriptase / Telomerase-associated protein of 45 kDa / La-related protein 7 homolog Similarity search - Component
Biological species
Tetrahymena thermophila (eukaryote)
Method
single particle reconstruction / cryo EM / Resolution: 3.5 Å
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
R35GM131901
United States
National Science Foundation (NSF, United States)
MCB2016540
United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
R01GM071940
United States
Citation
Journal: Nature / Year: 2022 Title: Structure of Tetrahymena telomerase-bound CST with polymerase α-primase. Authors: Yao He / He Song / Henry Chan / Baocheng Liu / Yaqiang Wang / Lukas Sušac / Z Hong Zhou / Juli Feigon / Abstract: Telomeres are the physical ends of linear chromosomes. They are composed of short repeating sequences (such as TTGGGG in the G-strand for Tetrahymena thermophila) of double-stranded DNA with a single- ...Telomeres are the physical ends of linear chromosomes. They are composed of short repeating sequences (such as TTGGGG in the G-strand for Tetrahymena thermophila) of double-stranded DNA with a single-strand 3' overhang of the G-strand and, in humans, the six shelterin proteins: TPP1, POT1, TRF1, TRF2, RAP1 and TIN2. TPP1 and POT1 associate with the 3' overhang, with POT1 binding the G-strand and TPP1 (in complex with TIN2) recruiting telomerase via interaction with telomerase reverse transcriptase (TERT). The telomere DNA ends are replicated and maintained by telomerase, for the G-strand, and subsequently DNA polymerase α-primase (PolαPrim), for the C-strand. PolαPrim activity is stimulated by the heterotrimeric complex CTC1-STN1-TEN1 (CST), but the structural basis of the recruitment of PolαPrim and CST to telomere ends remains unknown. Here we report cryo-electron microscopy (cryo-EM) structures of Tetrahymena CST in the context of the telomerase holoenzyme, in both the absence and the presence of PolαPrim, and of PolαPrim alone. Tetrahymena Ctc1 binds telomerase subunit p50, a TPP1 orthologue, on a flexible Ctc1 binding motif revealed by cryo-EM and NMR spectroscopy. The PolαPrim polymerase subunit POLA1 binds Ctc1 and Stn1, and its interface with Ctc1 forms an entry port for G-strand DNA to the POLA1 active site. We thus provide a snapshot of four key components that are required for telomeric DNA synthesis in a single active complex-telomerase-core ribonucleoprotein, p50, CST and PolαPrim-that provides insights into the recruitment of CST and PolαPrim and the handoff between G-strand and C-strand synthesis.
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