ArticleBiochemistry2011
Schizosaccharomyces pombe protection of telomeres 1 utilizes alternate binding modes to accommodate different telomeric sequences.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed.
- Structural insights into Pot1-ssDNA, Pot1-Tpz1 and Tpz1-Ccq1 Interactions within fission yeast shelterin complex.PLoS genetics · 2022Article
- Graphene oxide and fluorescent aptamer based novel biosensor for detection of 25-hydroxyvitamin DScientific reports · 2021Article
- A comparative study of protein-ssDNA interactions.NAR genomics and bioinformatics · 2021Article
- Structure, stability and specificity of the binding of ssDNA and ssRNA with proteins.PLoS computational biology · 2019Article
- Discrimination against RNA Backbones by a ssDNA Binding Protein.Structure (London, England : 1993) · 2018Article
- Human CST Prefers G-Rich but Not Necessarily Telomeric Sequences.Biochemistry · 2017Article
- Tying up the Ends: Plasticity in the Recognition of Single-Stranded DNA at Telomeres.Biochemistry · 2016Article
- Telomerase RNA stem terminus element affects template boundary element function, telomere sequence, and shelterin binding.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The OB-fold domain 1 of human POT1 recognizes both telomeric and non-telomeric DNA motifs.Biochimie · 2015Article
- The telomeric protein Pot1 from Schizosaccharomyces pombe binds ssDNA in two modes with differing 3' end availability.Nucleic acids research · 2014Article
- The tenacious recognition of yeast telomere sequence by Cdc13 is fully exerted by a single OB-fold domain.Nucleic acids research · 2014Article
- Single-stranded DNA-binding proteins: multiple domains for multiple functions.Structure (London, England : 1993) · 2013Review
- Finding the end: recruitment of telomerase to telomeres.Nature reviews. Molecular cell biology · 2013Review
- Nonspecific recognition is achieved in Pot1pC through the use of multiple binding modes.Structure (London, England : 1993) · 2013Article
- Practical strategies for the evaluation of high-affinity protein/nucleic acid interactions.Journal of nucleic acids investigation · 2013Article
- A small molecule inhibitor of Pot1 binding to telomeric DNA.Biochemistry · 2012Article
- Telomerase and telomere-associated proteins: structural insights into mechanism and evolution.Structure (London, England : 1993) · 2012Review
- DNA-induced dimerization of the single-stranded DNA binding telomeric protein Pot1 from Schizosaccharomyces pombe.Nucleic acids research · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
The ends of eukaryotic chromosomes consist of long tracts of repetitive GT-rich DNA with variable sequence homogeneity between and within organisms. Telomeres terminate in a conserved 3'-ssDNA overhang that, regardless of sequence variability, is specifically and tightly bound by proteins of the telomere-end protection family. The high affinity ssDNA-binding activity of S. pombe Pot1 protein (SpPot1) is conferred by a DNA-binding domain consisting of two subdomains, Pot1pN and Pot1pC. Previous work has shown that Pot1pN binds a single repeat of the core telomere sequence (GGTTAC) with exquisite specificity, while Pot1pC binds an extended sequence of nine nucleotides (GGTTACGGT) with modest specificity requirements. We find that full-length SpPot1 binds the composite 15mer, (GGTTAC)(2)GGT, and a shorter two-repeat 12mer, (GGTTAC)(2), with equally high affinity (<3 pM), but with substantially different kinetic and thermodynamic properties. The binding mode of the SpPot1/15mer complex is more stable than that of the 12mer complex, with a 2-fold longer half-life and increased tolerance to nucleotide and amino acid substitutions. Our data suggest that SpPot1 protection of heterogeneous telomeres is mediated through 5'-sequence recognition and the use of alternate binding modes to maintain high affinity interaction with the G-strand, while simultaneously discriminating against the complementary strand.
Indexed as
Identifiers
What OpenQuestion holds
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.