Evidence map›Paper›PMID 23610127›Full record

ArticleRNA (New York, N.Y.)2013

RNA recognition by the DNA end-binding Ku heterodimer.

Andrew B Dalby, Karen J Goodrich, Jennifer S Pfingsten, Thomas R Cech

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2013. 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
1.3field-weighted citation impact, top 19% 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, 32 citations in OpenAlex.

  1. Review
  2. Article
  3. How RNA impacts DNA repair.DNA repair · 2023
    Review
  4. Review
  5. CCAR2 functions downstream of the Shieldin complex to promote double-strand break end-joining.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
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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

4 authors at 1 institution in 1 country.

Andrew B DalbyHoward Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Colorado BioFrontiers Institute, Boulder, Colorado 80309-0596, USA.
Karen J Goodrich
Jennifer S Pfingsten
Thomas R Cech
Howard Hughes Medical Institute · US

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Most nucleic acid-binding proteins selectively bind either DNA or RNA, but not both nucleic acids. The Saccharomyces cerevisiae Ku heterodimer is unusual in that it has two very different biologically relevant binding modes: (1) Ku is a sequence-nonspecific double-stranded DNA end-binding protein with prominent roles in nonhomologous end-joining and telomeric capping, and (2) Ku associates with a specific stem-loop of TLC1, the RNA subunit of budding yeast telomerase, and is necessary for proper nuclear localization of this ribonucleoprotein enzyme. TLC1 RNA-binding and dsDNA-binding are mutually exclusive, so they may be mediated by the same site on Ku. Although dsDNA binding by Ku is well studied, much less is known about what features of an RNA hairpin enable specific recognition by Ku. To address this question, we localized the Ku-binding site of the TLC1 hairpin with single-nucleotide resolution using phosphorothioate footprinting, used chemical modification to identify an unpredicted motif within the hairpin secondary structure, and carried out mutagenesis of the stem-loop to ascertain the critical elements within the RNA that permit Ku binding. Finally, we provide evidence that the Ku-binding site is present in additional budding yeast telomerase RNAs and discuss the possibility that RNA binding is a conserved function of the Ku heterodimer.

Indexed as

Base SequenceBinding SitesCell NucleusCME-CarbodiimideDNA-Binding ProteinsDNA FootprintingElectrophoresis, Polyacrylamide GelInverted Repeat SequencesMutationNucleic Acid ConformationNucleotide MotifsPhosphorothioate OligonucleotidesProtein Interaction MappingRNARNA-Binding ProteinsRNA Cleavage1-cyclohexyl-3-(2-(4-morpholinyl)ethyl)carbodiimideCME-Carbodiimidedimethyl sulfateDNA-Binding Proteinshigh affinity DNA-binding factor, S cerevisiaePhosphorothioate OligonucleotidesRNARNA-Binding ProteinsRNA, FungalSaccharomyces cerevisiae ProteinsSulfuric Acid EstersTelomerasetelomerase RNAchemical modificationfootprintingKu heterodimerRNA bindingtelomerase

Identifiers

PMID23610127
PMCPMC3683917
OpenAlexW2156925994

What OpenQuestion holds

Textmetadata
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.