Evidence map›Paper›PMID 19395381›Full record

ArticleThe Journal of biological chemistry2009

Dual nuclease and helicase activities of Helicobacter pylori AddAB are required for DNA repair, recombination, and mouse infectivity.

Susan K Amundsen, Jutta Fero, Nina R Salama, Gerald R Smith

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

17 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
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  15. Review
  16. Recombination and DNA repair in Helicobacter pylori.Annual review of microbiology · 2011
    Review
  17. 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

4 authors at 2 institutions in 1 country.

Susan K AmundsenFrom the Divisions of Basic Sciences, Seattle, Washington 98109.
Jutta FeroHuman Biology, Fred Hutchinson Cancer Research Center, Seattle, Washington 98109.
Nina R SalamaHuman Biology, Fred Hutchinson Cancer Research Center, Seattle, Washington 98109.
Gerald R SmithFrom the Divisions of Basic Sciences, Seattle, Washington 98109. Electronic address: gsmith@fhcrc.org.
Fred Hutch Cancer Center · USOffice of Basic Energy Sciences · US

Funding

MOLECULAR ANALYSIS OF HOTSPOTS OF GENETIC RECOMBINATIONR01GM031693 · NIGMS · FRED HUTCHINSON CANCER RESEARCH CENTER · PI SMITH, GERALD R · 1985 to 2015
$9.7M
GENETIC REQUIREMENTS OF HELICOBACTER PYLORI INFECTIONR01AI054423 · NIAID · FRED HUTCHINSON CANCER RESEARCH CENTER · PI Nina Salama · 2004 to 2026
$9.5M
Molecular Analysis of Hotspots of Genetic RecombinationR56GM031693 · NIGMS · FRED HUTCHINSON CANCER RESEARCH CENTER · PI SMITH, GERALD R · 2007 to 2007
$586k
NIAID NIH HHS AI054423NIAID NIH HHS R01 AI054423NIGMS NIH HHS GM031693NIGMS NIH HHS R01 GM031693NIGMS NIH HHS R56 GM031693
6 · The paper itself

Abstract

Helicobacter pylori infection of the human stomach is associated with disease-causing inflammation that elicits DNA damage in both bacterial and host cells. Bacteria must repair their DNA to persist. The H. pylori AddAB helicase-exonuclease is required for DNA repair and efficient stomach colonization. To dissect the role of each activity in DNA repair and infectivity, we altered the AddA and AddB nuclease (NUC) domains and the AddA helicase (HEL) domain by site-directed mutagenesis. Extracts of Escherichia coli expressing H. pylori addA(NUC)B or addAB(NUC) mutants unwound DNA but had approximately half of the exonuclease activity of wild-type AddAB; the addA(NUC)B(NUC) double mutant lacked detectable nuclease activity but retained helicase activity. Extracts with AddA(HEL)B lacked detectable helicase and nuclease activity. H. pylori with the single nuclease domain mutations were somewhat less sensitive to the DNA-damaging agent ciprofloxacin than the corresponding deletion mutant, suggesting that residual nuclease activity promotes limited DNA repair. The addA(NUC) and addA(HEL) mutants colonized the stomach less efficiently than the wild type; addB(NUC) showed partial attenuation. E. coli DeltarecBCD expressing H. pylori addAB was recombination-deficient unless H. pylori recA was also expressed, suggesting a species-specific interaction between AddAB and RecA and also that H. pylori AddAB participates in both DNA repair and recombination. These results support a role for both the AddAB nuclease and helicase in DNA repair and promoting infectivity.

Indexed as

DNA HelicasesExodeoxyribonuclease VHelicobacter pyloriAnimalsAnti-Bacterial AgentsCiprofloxacinDNA, BacterialDNA RepairEscherichia coliExodeoxyribonucleasesFemaleHumansMiceMice, Inbred C57BLMutagenesis, Site-DirectedProtein Structure, TertiaryAddAB enzymeAnti-Bacterial AgentsCiprofloxacinDNA, BacterialDNA HelicasesExodeoxyribonucleasesExodeoxyribonuclease VRecombinant Proteins

Identifiers

PMID19395381
PMCPMC2719311
OpenAlexW2024327795

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.