ArticleThe Journal of biological chemistry2013
A conserved motif in Tetrahymena thermophila telomerase reverse transcriptase is proximal to the RNA template and is essential for boundary definition.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 13 citations in OpenAlex.
- Telomerase structural biology comes of age.Current opinion in structural biology · 2022Review
- Crystal structures of N-terminally truncated telomerase reverse transcriptase from fungi‡.Nucleic acids research · 2021Article
- Article
- A structurally conserved human andProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Structure of Telomerase with Telomeric DNA.Cell · 2018Article
- Hidden Structural Modules in a Cooperative RNA Folding Transition.Cell reports · 2018Article
- Current Perspectives of Telomerase Structure and Function in Eukaryotes with Emerging Views on Telomerase in Human Parasites.International journal of molecular sciences · 2018Review
- Progress in Human and Tetrahymena Telomerase Structure Determination.Annual review of biophysics · 2017Review
- Evolutionary perspectives of telomerase RNA structure and function.RNA biology · 2016Review
- Protein-RNA interaction restricts telomerase from running through the stop sign.Nature structural & molecular biology · 2015Article
- Structural basis of template-boundary definition in Tetrahymena telomerase.Nature structural & molecular biology · 2015Article
- DAZAP1 regulates the splicing of Crem, Crisp2 and Pot1a transcripts.Nucleic acids research · 2013Article
- A motif in the vertebrate telomerase N-terminal linker of TERT contributes to RNA binding and telomerase activity and processivity.Structure (London, England : 1993) · 2013Article
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
Abstract
The ends of linear chromosomes are extended by telomerase, a ribonucleoprotein complex minimally consisting of a protein subunit called telomerase reverse transcriptase (TERT) and the telomerase RNA (TER). TERT functions by reverse transcribing a short template region of TER into telomeric DNA. Proper assembly of TERT and TER is essential for telomerase activity; however, a detailed understanding of how TERT interacts with TER is lacking. Previous studies have identified an RNA binding domain (RBD) within TERT, which includes three evolutionarily conserved sequence motifs: CP2, CP, and T. Here, we used site-directed hydroxyl radical probing to directly identify sites of interaction between the TERT RBD and TER, revealing that the CP2 motif is in close proximity to a conserved region of TER known as the template boundary element (TBE). Gel shift assays on CP2 mutants confirmed that the CP2 motif is an RNA binding determinant. Our results explain previous work that established that mutations to the CP2 motif of TERT and to the TBE of TER both permit misincorporation of nucleotides into the growing DNA strand beyond the canonical template. Taken together, these results suggest a model in which the CP2 motif binds the TBE to strictly define which TER nucleotides can be reverse transcribed.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.