Evidence map›Paper›PMID 19920138›Full record

ArticleThe Journal of biological chemistry2010

Characterization of the mycobacterial AdnAB DNA motor provides insights into the evolution of bacterial motor-nuclease machines.

Mihaela-Carmen Unciuleac, Stewart Shuman

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.4field-weighted citation impact, top 22% 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

27 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
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  4. Clutch mechanism of chemomechanical coupling in a DNA resecting motor nuclease.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  5. Article
  6. Article
  7. How Does a Helicase Unwind DNA? Insights from RecBCD Helicase.BioEssays : news and reviews in molecular, cellular and developmental biology · 2018
    Review
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  16. On the mechanism of recombination hotspot scanning during double-stranded DNA break resection.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  17. Article
  18. Review
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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

2 authors at 1 institution in 1 country.

Mihaela-Carmen UnciuleacMolecular Biology Program, Sloan-Kettering Institute, New York, New York 10065, USA.
Stewart Shuman
Kettering University · US

Funding

Novel pathway of DNA inter-strand crosslink repair in mycobacteriaR01AI064693 · NIAID · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Michael S Glickman, Stewart H Shuman · 2005 to 2026
$11.1M
NIAID NIH HHS AI64693NIAID NIH HHS R01 AI064693
6 · The paper itself

Abstract

Mycobacterial AdnAB exemplifies a family of heterodimeric motor-nucleases involved in processing DNA double strand breaks (DSBs). The AdnA and AdnB subunits are each composed of an N-terminal UvrD-like motor domain and a C-terminal RecB-like nuclease module. Here we conducted a biochemical characterization of the AdnAB motor, using a nuclease-inactivated heterodimer. AdnAB is a vigorous single strand DNA (ssDNA)-dependent ATPase (k(cat) 415 s(-1)), and the affinity of the motor for the ssDNA cofactor increases 140-fold as DNA length is extended from 12 to 44 nucleotides. Using a streptavidin displacement assay, we demonstrate that AdnAB is a 3' --> 5' translocase on ssDNA. AdnAB binds stably to DSB ends. In the presence of ATP, the motor unwinds the DNA duplex without requiring an ssDNA loading strand. We integrate these findings into a model of DSB unwinding in which the "leading" AdnB and "lagging" AdnA motor domains track in tandem, 3' to 5', along the same DNA single strand. This contrasts with RecBCD, in which the RecB and RecD motors track in parallel along the two separated DNA single strands. The effects of 5' and 3' terminal obstacles on ssDNA cleavage by wild-type AdnAB suggest that the AdnA nuclease receives and processes the displaced 5' strand, while the AdnB nuclease cleaves the displaced 3' strand. We present evidence that the distinctive "molecular ruler" function of the ATP-dependent single strand DNase, whereby AdnAB measures the distance from the 5'-end to the sites of incision, reflects directional pumping of the ssDNA through the AdnAB motor into the AdnB nuclease. These and other findings suggest a scenario for the descent of the RecBCD- and AddAB-type DSB-processing machines from an ancestral AdnAB-like enzyme.

Indexed as

Evolution, MolecularAdenosine TriphosphatasesBacterial ProteinsDNA Breaks, Double-StrandedDNA HelicasesDNA RepairDNA, Single-StrandedMutagenesis, Site-DirectedMycobacterium smegmatisProtein BindingProtein Structure, TertiaryRecombinant ProteinsAdenosine TriphosphatasesBacterial ProteinsDNA HelicasesDNA, Single-StrandedRecombinant Proteinssingle stranded DNA dependent ATPase

Identifiers

PMID19920138
PMCPMC2807320
OpenAlexW2012095700

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.