ArticleNucleic acids research2010
The N-terminus of hTERT contains a DNA-binding domain and is required for telomerase activity and cellular immortalization.
Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
30 citing papers in PubMed, 53 citations in OpenAlex.
- Computational Identification and Illustrative Standard for Representation of Unimolecular G-Quadruplex Secondary Structures (CIIS-GQ).Journal of computer-aided molecular design · 2024Article
- Comprehensive Characterization and Global Transcriptome Analysis of Human Fetal Liver Terminal Erythropoiesis.Genomics, proteomics & bioinformatics · 2023Article
- Orchestrating nucleic acid-protein interactions at chromosome ends: telomerase mechanisms come into focus.Nature structural & molecular biology · 2023Review
- Many Functions of Telomerase Components: Certainties, Doubts, and Inconsistencies.International journal of molecular sciences · 2022Review
- Structural basis of human telomerase recruitment by TPP1-POT1.Science (New York, N.Y.) · 2022Article
- Observation of processive telomerase catalysis using high-resolution optical tweezers.Nature chemical biology · 2020Article
- Direct observation of nucleic acid binding dynamics by the telomerase essential N-terminal domain.Nucleic acids research · 2018Article
- Structure and function of the N-terminal domain of the yeast telomerase reverse transcriptase.Nucleic acids research · 2018Article
- Tandem affinity purification of AtTERT reveals putative interaction partners of plant telomerase in vivo.Protoplasma · 2017Article
- Telomerase Regulation from Beginning to the End.Genes · 2016Review
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- Human telomerase specialization for repeat synthesis by unique handling of primer-template duplex.The EMBO journal · 2014Article
- Telomere repeat binding proteins are functional components of Arabidopsis telomeres and interact with telomerase.The Plant journal : for cell and molecular biology · 2014Article
- A yeast chemical genetic screen identifies inhibitors of human telomerase.Chemistry & biology · 2013Article
- Prognostic role of telomerase activity in gastric adenocarcinoma: A meta-analysis.Experimental and therapeutic medicine · 2012Article
- Native gel electrophoresis of human telomerase distinguishes active complexes with or without dyskerin.Nucleic acids research · 2012Article
- Long telomeres bypass the requirement for telomere maintenance in human tumorigenesis.Cell reports · 2012Article
- Dyskeratosis congenita as a disorder of telomere maintenance.Mutation research · 2012Review
- It all comes together at the ends: telomerase structure, function, and biogenesis.Mutation research · 2012Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Telomerase defers the onset of telomere damage-induced signaling and cellular senescence by adding DNA onto chromosome ends. The ability of telomerase to elongate single-stranded telomeric DNA depends on the reverse transcriptase domain of TERT, and also relies on protein:DNA contacts outside the active site. We purified the N-terminus of human TERT (hTEN) from Escherichia coli, and found that it binds DNA with a preference for telomeric sequence of a certain length and register. hTEN interacted with the C-terminus of hTERT in trans to reconstitute enzymatic activity in vitro. Mutational analysis of hTEN revealed that amino acids Y18 and Q169 were required for telomerase activity in vitro, but not for the interaction with telomere DNA or the C-terminus. These mutants did not reconstitute telomerase activity in cells, maintain telomere length, or extend cellular lifespan. In addition, we found that T116/T117/S118, while dispensable in vitro, were required for cellular immortalization. Thus, the interactions of hTEN with telomere DNA and the C-terminus of hTERT are functionally separable from the role of hTEN in telomere elongation activity in vitro and in vivo, suggesting other roles for the protein and nucleic acid interactions of hTEN within, and possibly outside, the telomerase catalytic core.
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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.