Evidence map›Paper›PMID 33958590›Full record

ArticleNature communications2021

Structural coordination between active sites of a CRISPR reverse transcriptase-integrase complex.

Joy Y Wang, Christopher M Hoel, Basem Al-Shayeb, Jillian F Banfield, Stephen G Brohawn, Jennifer A Doudna

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

15 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Reverse transcriptases prime DNA synthesis.Nucleic acids research · 2023
    Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Review
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 2 institutions in 1 country.

Joy Y WangDepartment of Chemistry, University of California, Berkeley, Berkeley, CA, USA.
Christopher M HoelCalifornia Institute for Quantitative Biosciences, University of California, Berkeley, Berkeley, CA, USA.ORCID http://orcid.org/0000-0002-1344-0780
Basem Al-ShayebCalifornia Institute for Quantitative Biosciences, University of California, Berkeley, Berkeley, CA, USA.
Jillian F BanfieldDepartment of Plant and Microbial Biology, University of California, Berkeley, Berkeley, CA, USA.ORCID http://orcid.org/0000-0001-8203-8771
Stephen G BrohawnCalifornia Institute for Quantitative Biosciences, University of California, Berkeley, Berkeley, CA, USA.ORCID http://orcid.org/0000-0001-6768-3406
Jennifer A DoudnaDepartment of Chemistry, University of California, Berkeley, Berkeley, CA, USA. doudna@berkeley.edu.ORCID http://orcid.org/0000-0001-9161-999X
QB3 · USPlanetary Science Institute · US

Funding

New approaches to understanding biological force sensationDP2GM123496 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI BROHAWN, STEPHEN GRAF · 2016 to 2016
$2.4M
Howard Hughes Medical InstituteNIGMS NIH HHS DP2 GM123496
6 · The paper itself

Abstract

CRISPR-Cas systems provide adaptive immunity in bacteria and archaea, beginning with integration of foreign sequences into the host CRISPR genomic locus and followed by transcription and maturation of CRISPR RNAs (crRNAs). In some CRISPR systems, a reverse transcriptase (RT) fusion to the Cas1 integrase and Cas6 maturase creates a single protein that enables concerted sequence integration and crRNA production. To elucidate how the RT-integrase organizes distinct enzymatic activities, we present the cryo-EM structure of a Cas6-RT-Cas1-Cas2 CRISPR integrase complex. The structure reveals a heterohexamer in which the RT directly contacts the integrase and maturase domains, suggesting functional coordination between all three active sites. Together with biochemical experiments, our data support a model of sequential enzymatic activities that enable CRISPR sequence acquisition from RNA and DNA substrates. These findings highlight an expanded capacity of some CRISPR systems to acquire diverse sequences that direct CRISPR-mediated interference.

Indexed as

CRISPR-Cas SystemsCatalytic DomainCRISPR-Associated ProteinsCryoelectron MicroscopyEndonucleasesEscherichia coliIntegrasesPiscirickettsiaceaeRecombinant ProteinsRNA-Directed DNA PolymeraseCRISPR-Associated ProteinsEndonucleasesIntegrasesRecombinant ProteinsRNA-Directed DNA Polymerase

Identifiers

PMID33958590
PMCPMC8102632
OpenAlexW3157575462

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.