ArticleNucleic acids research2007
Modeling and structure function analysis of the putative anchor site of yeast telomerase.
Article in Nucleic acids research, 2007. 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.
- Cryo-electron microscopy structure of the budding yeast telomerase holoenzyme.Science (New York, N.Y.) · 2026Article
- Orchestrating nucleic acid-protein interactions at chromosome ends: telomerase mechanisms come into focus.Nature structural & molecular biology · 2023Review
- Telomere DNA G-quadruplex folding within actively extending human telomerase.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Direct observation of nucleic acid binding dynamics by the telomerase essential N-terminal domain.Nucleic acids research · 2018Article
- Regulated assembly and disassembly of the yeast telomerase quaternary complex.Genes & development · 2014Article
- A mutation in the catalytic subunit of yeast telomerase alters primer-template alignment while promoting processivity and protein-DNA binding.Journal of cell science · 2011Article
- Direct involvement of the TEN domain at the active site of human telomerase.Nucleic acids research · 2011Article
- InTERTpreting telomerase structure and function.Nucleic acids research · 2010Review
- The N-terminus of hTERT contains a DNA-binding domain and is required for telomerase activity and cellular immortalization.Nucleic acids research · 2010Article
- Plasticity of telomere maintenance mechanisms in yeast.Trends in biochemical sciences · 2010Review
- Human telomerase reverse transcriptase (hTERT) Q169 is essential for telomerase function in vitro and in vivo.PloS one · 2009Article
- Mutation in TERT separates processivity from anchor-site function.Nature structural & molecular biology · 2008Article
- Yeast Est2p affects telomere length by influencing association of Rap1p with telomeric chromatin.Molecular and cellular biology · 2008Article
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Authors and funding
2 authors.
Funding
Abstract
Telomerase is a ribonucleoprotein reverse transcriptase responsible for extending one strand of the telomere terminal repeats. Unique among reverse transcriptases, telomerase is thought to possess a DNA-binding domain (known as anchor site) that allows the enzyme to add telomere repeats processively. Previous crosslinking and mutagenesis studies have mapped the anchor site to an N-terminal region of TERT, and the structure of this region of Tetrahymena TERT was recently determined at atomic resolutions. Here we use a combination of homology modeling, electrostatic calculation and site-specific mutagenesis analysis to identify a positively charged, functionally important surface patch on yeast TERT. This patch is lined by both conserved and non-conserved residues, which when mutated, caused loss of telomerase processivity in vitro and telomere shortening in vivo. In addition, we demonstrate that a point mutation in this domain of yeast TERT simultaneously enhanced the repeat addition processivity of telomerase and caused telomere elongation. Our data argue that telomerase anchor site has evolved species-specific residues to interact with species-specific telomere repeats. The data also reinforce the importance of telomerase processivity in regulating telomere length.
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