ArticleThe Journal of biological chemistry2017
Shared Subunits of Tetrahymena Telomerase Holoenzyme and Replication Protein A Have Different Functions in Different Cellular Complexes.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 29 citations in OpenAlex.
- Fission yeast RPA-TERT-Tpz1TPP1 complex promotes telomere extension and suppresses telomere recombination.PLoS genetics · 2026Article
- Fission yeast RPA-TERT-Tpz1bioRxiv : the preprint server for biology · 2026Article
- Human RPA is an essential telomerase processivity factor for maintaining telomeres.Science (New York, N.Y.) · 2025Article
- The canonical RPA complex interacts with Est3 to regulate yeast telomerase activity.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- RPA-like single-stranded DNA-binding protein complexes including CST serve as specialized processivity factors for polymerases.Current opinion in structural biology · 2023Review
- Proteomic analysis defines the interactome of telomerase in the protozoan parasite,Frontiers in cell and developmental biology · 2023Article
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- A structurally conserved human andProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Functional Diversification of Replication Protein A Paralogs and Telomere Length Maintenance in Arabidopsis.Genetics · 2020Article
- Structural Biology of Telomerase.Cold Spring Harbor perspectives in biology · 2019Review
- TIN2 Functions with TPP1/POT1 To Stimulate Telomerase Processivity.Molecular and cellular biology · 2019Article
- Functional Proteomics of Nuclear Proteins inGenes · 2019Review
- Telomerase structures and regulation: shedding light on the chromosome end.Current opinion in structural biology · 2019Review
- Evolutionary rates of mammalian telomere-stability genes correlate with karyotype features and female germline expression.Nucleic acids research · 2018Article
- Structure of Telomerase with Telomeric DNA.Cell · 2018Article
- Structural biology of telomerase and its interaction at telomeres.Current opinion in structural biology · 2017Review
- Telomerase Mechanism of Telomere Synthesis.Annual review of biochemistry · 2017Review
- Progress in Human and Tetrahymena Telomerase Structure Determination.Annual review of biophysics · 2017Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
In most eukaryotes, telomere maintenance relies on telomeric repeat synthesis by a reverse transcriptase named telomerase. To synthesize telomeric repeats, the catalytic subunit telomerase reverse transcriptase (TERT) uses the RNA subunit (TER) as a template. In the ciliate Tetrahymena thermophila, the telomerase holoenzyme consists of TER, TERT, and eight additional proteins, including the telomeric repeat single-stranded DNA-binding protein Teb1 and its heterotrimer partners Teb2 and Teb3. Teb1 is paralogous to the large subunit of the general single-stranded DNA binding heterotrimer replication protein A (RPA). Little is known about the function of Teb2 and Teb3, which are structurally homologous to the RPA middle and small subunits, respectively. Here, epitope-tagging Teb2 and Teb3 expressed at their endogenous gene loci enabled affinity purifications that revealed that, unlike other Tetrahymena telomerase holoenzyme subunits, Teb2 and Teb3 are not telomerase-specific. Teb2 and Teb3 assembled into other heterotrimer complexes, which when recombinantly expressed had the general single-stranded DNA binding activity of RPA complexes, unlike the telomere-specific DNA binding of Teb1 or the TEB heterotrimer of Teb1, Teb2, and Teb3. TEB had no more DNA binding affinity than Teb1 alone. In contrast, heterotrimers reconstituted with Teb2 and Teb3 and two other Tetrahymena RPA large subunit paralogs had higher DNA binding affinity than their large subunit alone. Teb1 and TEB, but not RPA, increased telomerase processivity. We conclude that in the telomerase holoenzyme, instead of binding DNA, Teb2 and Teb3 are Teb1 assembly factors. These findings demonstrate that Tetrahymena telomerase holoenzyme and RPA complexes share subunits and that RPA subunits have distinct functions in different heterotrimer assemblies.
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