ArticleBiochemistry2017
Human CST Prefers G-Rich but Not Necessarily Telomeric Sequences.
Article in Biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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
46 citing papers in PubMed.
- Mechanisms and disease relevance of DNA break repair pathway choice.Nature reviews. Molecular cell biology · 2026Review
- Distinct ATRX functions cooperate with 9-1-1 and CST complexes to safeguard replication and telomere integrity.Nature structural & molecular biology · 2026Article
- Conditional deletion of human STN1 leads to telomere dysfunction, genome instability and proliferation defects.Journal of cell science · 2026Article
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- STN1 facilitates metastasis by promoting transcription of EMT-activator ZEB1 in pancreatic cancer.Nature communications · 2025Article
- CTC1-STN1-TEN1 controls DNA break repair pathway choice via DNA end resection blockade.Science (New York, N.Y.) · 2025Article
- Human CST Stimulates Base Excision Repair to Prevent the Accumulation of Oxidative DNA Damage.Journal of molecular biology · 2024Article
- Article
- Guardians of the Genome: How the Single-Stranded DNA-Binding Proteins RPA and CST Facilitate Telomere Replication.Biomolecules · 2024Review
- Telomere C-Strand Fill-In Machinery: New Insights into the Human CST-DNA Polymerase Alpha-Primase Structures and Functions.Sub-cellular biochemistry · 2024Review
- POT1 recruits and regulates CST-Polα/Primase at human telomeres.bioRxiv : the preprint server for biology · 2023Article
- Models for human telomere C-strand fill-in by CST-Polα-primase.Trends in biochemical sciences · 2023Review
- RPA-like single-stranded DNA-binding protein complexes including CST serve as specialized processivity factors for polymerases.Current opinion in structural biology · 2023Review
- CST-Polα/Primase: the second telomere maintenance machine.Genes & development · 2023Review
- RPA engages telomeric G-quadruplexes more effectively than CST.Nucleic acids research · 2023Article
- CST/Polα/primase-mediated fill-in synthesis at DSBs.Cell cycle (Georgetown, Tex.) · 2023Article
- Replication Protein A Utilizes Differential Engagement of Its DNA-Binding Domains to Bind Biologically Relevant ssDNAs in Diverse Binding Modes.Biochemistry · 2022Article
- Transcriptomic Analysis of Conserved Telomere Maintenance Component 1 (CTC1) and Its Association with Leukemia.Journal of clinical medicine · 2022Article
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Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The human CST (CTC1-STN1-TEN1) heterotrimeric complex plays roles in both telomere maintenance and DNA replication through its ability to interact with single-stranded DNA (ssDNA) of a variety of sequences. The precise sequence specificity required to execute these functions is unknown. Telomere-binding proteins have been shown to specifically recognize key telomeric sequence motifs within ssDNA while accommodating nonspecifically recognized sequences through conformationally plastic interfaces. To better understand the role CST plays in these processes, we have produced a highly purified heterotrimer and elucidated the sequence requirements for CST recognition of ssDNA in vitro. CST discriminates against random sequence and binds a minimal ssDNA comprised of three repeats of telomeric sequence. Replacement of individual nucleotides with their complement reveals that guanines are specifically recognized in a largely additive fashion and that specificity is distributed uniformly throughout the ligand. Unexpectedly, adenosines are also well tolerated at these sites, but cytosines are disfavored. Furthermore, sequences unrelated to the telomere repeat, yet still G-rich, bind CST well. Thus, CST is not inherently telomere-specific, but rather is a G-rich sequence binder. This biochemical activity is reminiscent of the yeast t-RPA and Tetrahymena thermophila CST complexes and is consistent with roles at G-rich sites throughout the genome.
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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.