Evidence map›Paper›PMID 22954644›Full record

ReviewRNA biology2012

Cascade-mediated binding and bending of negatively supercoiled DNA.

Edze R Westra, Benedikt Nilges, Paul B G van Erp, John van der Oost, Remus T Dame, Stan J J Brouns

Open access · bronzeAbstract readReview
In one paragraph

Review in RNA biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

26 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. CRISPR-Cas Systems: A Functional Perspective and Innovations.International journal of molecular sciences · 2025
    Review
  3. Review
  4. Digging into the lesser-known aspects of CRISPR biology.International microbiology : the official journal of the Spanish Society for Microbiology · 2021
    Review
  5. Article
  6. Article
  7. Review
  8. Cas1 and the Csy complex are opposing regulators of Cas2/3 nuclease activity.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  9. Article
  10. CRISPR-Cas: biology, mechanisms and relevance.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2016
    Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Review
  16. Crystal structure of Thermobifida fusca Cse1 reveals target DNA binding site.Protein science : a publication of the Protein Society · 2015
    Article
  17. Molecular insights into DNA interference by CRISPR-associated nuclease-helicase Cas3.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  18. Review
  19. Molecular mechanisms of CRISPR-mediated microbial immunity.Cellular and molecular life sciences : CMLS · 2014
    Review
  20. 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

6 authors at 3 institutions in 3 countries.

Edze R WestraLaboratory of Microbiology, Department of Agrotechnology and Food Sciences, Wageningen University, The Netherlands. edze.westra@wur.nl
Benedikt Nilges
Paul B G van Erp
John van der Oost
Remus T Dame
Stan J J Brouns
Czech Academy of Sciences, Institute of Microbiology · CZLeiden University · NLWageningen University & Research · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Prokaryotes possess various defense mechanisms against invading DNA. Adaptive defense by CRISPR/Cas relies on incorporation of invader DNA sequences in the host genome. In Escherichia coli, processed transcripts of these incorporated sequences (crRNAs) guide Cascade-mediated invader DNA recognition. ( 1) (-) ( 4) Cascade is a multisubunit ribonucleoprotein complex, consisting of one crRNA and five proteins: Cse1, Cse2, Cas7, Cas5 and Cas6e. ( 1) (, ) ( 2) Cascade-mediated DNA recognition requires a conserved sequence adjacent to the target (protospacer adjacent motif, PAM) and a negatively supercoiled DNA topology. ( 3) (, ) ( 4) While Cse1 carries out PAM recognition, ( 5) the Cascade structure suggests that Cse2 may interact with target DNA in the PAM-distal end of the protospacer. ( 6) Using Electrophoretic Mobility Shift Assays, we here describe the function of the Cse1 and Cse2 subunits in the context of protospacer recognition on negatively supercoiled DNA. While Cse1 is required for nonspecific DNA binding, Cse2 appears to be important for specific binding, presumably by mediating stabilizing interactions with the displaced strand, the R-loop, or both. Furthermore, we performed Scanning Force Microscopy using linearized DNA molecules, which facilitates accurate and reliable measurements of Cascade-mediated bending. This analysis reveals that Cascade binding induces flexibility in the DNA target, most likely due to single stranded DNA regions flanking the R-loop.

Indexed as

Amino Acid MotifsDNA, BacterialDNA-Binding ProteinsDNA, SuperhelicalEscherichia coliEscherichia coli ProteinsRibonucleoproteinsDNA, BacterialDNA-Binding ProteinsDNA, SuperhelicalEscherichia coli ProteinsRibonucleoproteins

Identifiers

PMID22954644
PMCPMC3579878
OpenAlexW2091791718

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.