Evidence map›Paper›PMID 21911358›Full record

ArticleNucleic acids research2012

DNA-induced dimerization of the single-stranded DNA binding telomeric protein Pot1 from Schizosaccharomyces pombe.

Jayakrishnan Nandakumar, Thomas R Cech

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.2field-weighted citation impact, top 21% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. POT1-TPP1 binding stabilizes POT1, promoting efficient telomere maintenance.Computational and structural biotechnology journal · 2022
    Article
  5. Review
  6. POT1-TPP1 differentially regulates telomerase via POT1 His266 and as a function of single-stranded telomere DNA length.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. The oligonucleotide/oligosaccharide-binding fold motif is a poly(ADP-ribose)-binding domain that mediates DNA damage response.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  15. Article
  16. Article
  17. Finding the end: recruitment of telomerase to telomeres.Nature reviews. Molecular cell biology · 2013
    Review
  18. Article
  19. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

Jayakrishnan NandakumarDepartment of Chemistry and Biochemistry, Howard Hughes Medical Institute, University of Colorado, Boulder, CO 80309-0215, USA.
Thomas R Cech
Howard Hughes Medical Institute · USUniversity of Colorado Boulder · US

Funding

Telomerase and Telomeres: Structure, Function/RegulationR01GM028039 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI CECH, THOMAS ROBERT · 1985 to 2009
$2.6M
STUDIES OF NUCLEIC ACID STRUCTURE AND REACTIVITYR37GM028039 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI CECH, THOMAS R · 1988 to 1997
–
Howard Hughes Medical InstituteNIGMS NIH HHS GM28039
6 · The paper itself

Abstract

Eukaryotic chromosome ends are protected from illicit DNA joining by protein-DNA complexes called telomeres. In most studied organisms, telomeric DNA is composed of multiple short G-rich repeats that end in a single-stranded tail that is protected by the protein POT1. Mammalian POT1 binds two telomeric repeats as a monomer in a sequence-specific manner, and discriminates against RNA of telomeric sequence. While addressing the RNA discrimination properties of SpPot1, the POT1 homolog in Schizosaccharomyces pombe, we found an unanticipated ssDNA-binding mode in which two SpPot1 molecules bind an oligonucleotide containing two telomeric repeats. DNA binding seems to be achieved via binding of the most N-terminal OB domain of each monomer to each telomeric repeat. The SpPot1 dimer may have evolved to accommodate the heterogeneous spacers that occur between S. pombe telomeric repeats, and it also has implications for telomere architecture. We further show that the S. pombe telomeric protein Tpz1, like its mammalian homolog TPP1, increases the affinity of Pot1 for telomeric single-stranded DNA and enhances the discrimination of Pot1 against RNA.

Indexed as

Carrier ProteinsDimerizationDNA-Binding ProteinsDNA, Single-StrandedOligonucleotidesProtein Structure, TertiaryRepetitive Sequences, Nucleic AcidRNASchizosaccharomyces pombe ProteinsShelterin ComplexTelomereTelomere-Binding ProteinsThymidineUridineCarrier ProteinsDNA-Binding ProteinsDNA, Single-StrandedOligonucleotidespot1 protein, S pombeRNASchizosaccharomyces pombe ProteinsShelterin ComplexTelomere-Binding ProteinsThymidineTpz1 protein, S pombeUridine

Identifiers

PMID21911358
PMCPMC3245936
OpenAlexW2113933163

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

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.