Evidence map›Paper›PMID 33154402›Full record

ArticleScientific reports2020

Chi hotspot control of RecBCD helicase-nuclease by long-range intramolecular signaling.

Susan K Amundsen, Andrew F Taylor, Gerald R Smith

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

8 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. RecBCD enzyme: mechanistic insights from mutants of a complex helicase-nuclease.Microbiology and molecular biology reviews : MMBR · 2023
    Review
  7. Article
  8. 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

3 authors at 1 institution in 1 country.

Susan K AmundsenDivision of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, WA, USA.
Andrew F TaylorDivision of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, WA, USA.
Gerald R SmithDivision of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, WA, USA. gsmith@fredhutch.org.
Fred Hutch Cancer Center · US

Funding

Translational Bioimaging Core Shared ResourceP30CA015704 · NCI · FRED HUTCHINSON CANCER RESEARCH CENTER · PI Eric Collisson · 1985 to 2026
$296.4M
Molecular analysis of genetic recombination and DNA break repairR35GM118120 · NIGMS · FRED HUTCHINSON CANCER RESEARCH CENTER · PI SMITH, GERALD R · 2016 to 2025
$9.3M
NCI NIH HHS P30 CA015704NIGMS NIH HHS R35 GM118120
6 · The paper itself

Abstract

Repair of broken DNA by homologous recombination requires coordinated enzymatic reactions to prepare it for interaction with intact DNA. The multiple activities of enterobacterial RecBCD helicase-nuclease are coordinated by Chi recombination hotspots (5' GCTGGTGG 3') recognized during DNA unwinding. Chi is recognized in a tunnel in RecC but activates the RecB nuclease, > 25 Ǻ away. How the Chi-dependent signal travels this long distance has been unknown. We found a Chi hotspot-deficient mutant in the RecB helicase domain located > 45 Ǻ from both the Chi-recognition site and the nuclease active site. This unexpected observation led us to find additional mutations that reduced or eliminated Chi hotspot activity in each subunit and widely scattered throughout RecBCD. Each mutation alters the intimate contact between one or another pair of subunits in crystal or cryoEM structures of RecBCD bound to DNA. Collectively, these mutations span a path about 185 Ǻ long from the Chi recognition site to the nuclease active site. We discuss these surprising results in the context of an intramolecular signal transduction accounting for many previous observations.

Indexed as

Recombination, GeneticAmino Acid SequenceBinding SitesDNA, BacterialDNA HelicasesDNA RepairEndonucleasesEscherichia coliEscherichia coli ProteinsExodeoxyribonuclease VModels, MolecularMutationProtein Structure, QuaternarySignal TransductionDNA, BacterialDNA HelicasesEndonucleasesEscherichia coli ProteinsExodeoxyribonuclease Vexodeoxyribonuclease V, E coli

Identifiers

PMID33154402
PMCPMC7644769
OpenAlexW3096931281

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.