Evidence map›Paper›PMID 21343909›Full record

ArticleThe EMBO journal2011

Cas3 is a single-stranded DNA nuclease and ATP-dependent helicase in the CRISPR/Cas immune system.

Tomas Sinkunas, Giedrius Gasiunas, Christophe Fremaux, Rodolphe Barrangou, Philippe Horvath, Virginijus Siksnys

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 252 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
252citing papers in PubMed, 1 pooled it
14.4field-weighted citation impact, top 1% 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

252 citing papers in PubMed, 1 synthesis or guideline pooled it, 448 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Enhanced editing ofApplied and environmental microbiology · 2026
    Article
  13. Occurrence and applications of CRISPR-Cas systems in bifidobacteria.Applied and environmental microbiology · 2026
    Review
  14. CRISPR-Cas targeting inmicroLife · 2026
    Article
  15. Article
  16. Structural characterization of anti-CRISPR protein AcrIE9.Structural dynamics (Melville, N.Y.) · 2025
    Article
  17. Review
  18. Review
  19. Article
  20. D-CAPS: an efficient CRISPR-Cas9-based phage defense system forActa biochimica et biophysica Sinica · 2025
    Article

192 more citing papers are in PubMed but not listed here.

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.

Tomas SinkunasDepartment of Protein-DNA Interactions, Institute of Biotechnology, Vilnius University, Vilnius, Lithuania.
Giedrius Gasiunas
Christophe Fremaux
Rodolphe Barrangou
Philippe Horvath
Virginijus Siksnys
Vilnius University · LTDanaher (France) · FRMadison Group (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Clustered regularly interspaced short palindromic repeat (CRISPR) is a recently discovered adaptive prokaryotic immune system that provides acquired immunity against foreign nucleic acids by utilizing small guide crRNAs (CRISPR RNAs) to interfere with invading viruses and plasmids. In Escherichia coli, Cas3 is essential for crRNA-guided interference with virus proliferation. Cas3 contains N-terminal HD phosphohydrolase and C-terminal Superfamily 2 (SF2) helicase domains. Here, we provide the first report of the cloning, expression, purification and in vitro functional analysis of the Cas3 protein of the Streptococcus thermophilus CRISPR4 (Ecoli subtype) system. Cas3 possesses a single-stranded DNA (ssDNA)-stimulated ATPase activity, which is coupled to unwinding of DNA/DNA and RNA/DNA duplexes. Cas3 also shows ATP-independent nuclease activity located in the HD domain with a preference for ssDNA substrates. To dissect the contribution of individual domains, Cas3 separation-of-function mutants (ATPase(+)/nuclease(-) and ATPase(-)/nuclease(+)) were obtained by site-directed mutagenesis. We propose that the Cas3 ATPase/helicase domain acts as a motor protein, which assists delivery of the nuclease activity to Cascade-crRNA complex targeting foreign DNA.

Indexed as

Repetitive Sequences, Nucleic AcidAdenosine TriphosphateCloning, MolecularDNA, BacterialDNA HelicasesDNA Mutational AnalysisDNA, Single-StrandedEscherichia coliGene ExpressionModels, BiologicalMolecular Sequence DataMutagenesis, Site-DirectedPlasmidsSequence Analysis, DNAStreptococcus thermophilusAdenosine TriphosphateDNA, BacterialDNA HelicasesDNA, Single-Stranded

Identifiers

PMID21343909
PMCPMC3094125
OpenAlexW1926535993

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.