Evidence map›Paper›PMID 36543802›Full record

ArticleNature communications2022

Structure of a RecT/Redβ family recombinase in complex with a duplex intermediate of DNA annealing.

Brian J Caldwell, Andrew S Norris, Caroline F Karbowski, Alyssa M Wiegand, Vicki H Wysocki, Charles E Bell

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.4field-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

14 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Monomers and short oligomers of human RAD52 promote single-strand annealing.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Article
  10. A structural phylogenetic tree of Rad52 and its annealase superfamily.Computational and structural biotechnology journal · 2025
    Article
  11. Proof of ssDNA degraded from dsDNA for ET recombination.Biochemistry and biophysics reports · 2024
    Article
  12. Review
  13. Article
  14. 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 1 institution in 1 country.

Brian J CaldwellOhio State Biochemistry Program, The Ohio State University, Columbus, OH, 43210, USA.
Andrew S NorrisDepartment of Chemistry and Biochemistry and Resource for Native MS-Guided Structural Biology, The Ohio State University, Columbus, OH, 43210, USA.
Caroline F KarbowskiDepartment of Biological Chemistry and Pharmacology, The Ohio State University, Columbus, OH, 43210, USA.ORCID 0000-0002-1522-3333
Alyssa M WiegandDepartment of Biological Chemistry and Pharmacology, The Ohio State University, Columbus, OH, 43210, USA.
Vicki H WysockiOhio State Biochemistry Program, The Ohio State University, Columbus, OH, 43210, USA.ORCID 0000-0003-0495-2538
Charles E BellOhio State Biochemistry Program, The Ohio State University, Columbus, OH, 43210, USA. bell.489@osu.edu.ORCID 0000-0001-6486-9408
The Ohio State University · US

Funding

Waters Select Series Cyclic IMS for P41 Native MS Resource Application to Alzheimer's DiseaseP41GM128577 · NIGMS · OHIO STATE UNIVERSITY · PI WYSOCKI, VICKI H. · 2018 to 2022
$7.6M
Molecular Biophysics predoctoral training at The Ohio State UniversityT32GM118291 · NIGMS · OHIO STATE UNIVERSITY · PI BUNDSCHUH, RALF A, KURET, JEFF · 2017 to 2021
$720k
NIGMS NIH HHS P41 GM128577NIGMS NIH HHS T32 GM118291
6 · The paper itself

Abstract

Some bacteriophage encode a recombinase that catalyzes single-stranded DNA annealing (SSA). These proteins are apparently related to RAD52, the primary human SSA protein. The best studied protein, Redβ from bacteriophage λ, binds weakly to ssDNA, not at all to dsDNA, but tightly to a duplex intermediate of annealing formed when two complementary DNA strands are added to the protein sequentially. We used single particle cryo-electron microscopy (cryo-EM) to determine a 3.4 Å structure of a Redβ homolog from a prophage of Listeria innocua in complex with two complementary 83mer oligonucleotides. The structure reveals a helical protein filament bound to a DNA duplex that is highly extended and unwound. Native mass spectrometry confirms that the complex seen by cryo-EM is the predominant species in solution. The protein shares a common core fold with RAD52 and a similar mode of ssDNA-binding. These data provide insights into the mechanism of protein-catalyzed SSA.

Indexed as

DNARecombinasesCryoelectron MicroscopyDNA-Binding ProteinsDNA, Single-StrandedListeriaProphagesProtein BindingRad51 RecombinaseRad52 DNA Repair and Recombination ProteinDNADNA-Binding ProteinsDNA, Single-StrandedRad51 RecombinaseRad52 DNA Repair and Recombination ProteinRecombinases

Identifiers

PMID36543802
PMCPMC9772228
OpenAlexW4313340369

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.