Evidence map›Paper›PMID 24169816›Full record

ArticleMicrobiology (Reading, England)2014

Effects of conserved residues and naturally occurring mutations on Mycobacterium tuberculosis RecG helicase activity.

Ephrem Debebe Zegeye, Seetha V Balasingham, Jon K Laerdahl, Håvard Homberset, Per E Kristiansen, Tone Tønjum

Open access · greenAbstract read
In one paragraph

Article in Microbiology (Reading, England), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.4field-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

7 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. 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 2 institutions in 1 country.

Ephrem Debebe ZegeyeCentre for Molecular Biology and Neuroscience and Department of Microbiology, Oslo University Hospital (Rikshospitalet), Oslo, Norway.
Seetha V BalasinghamCentre for Molecular Biology and Neuroscience and Department of Microbiology, Oslo University Hospital (Rikshospitalet), Oslo, Norway.
Jon K LaerdahlBioinformatics Core Facility, Department of Informatics, University of Oslo, Oslo, Norway.
Håvard HombersetCentre for Molecular Biology and Neuroscience and Department of Microbiology, University of Oslo, Oslo, Norway.
Per E KristiansenDepartment of Molecular Biosciences, University of Oslo, Oslo, Norway.
Tone TønjumCentre for Molecular Biology and Neuroscience and Department of Microbiology, Oslo University Hospital (Rikshospitalet), Oslo, Norway.
University of Oslo · NOOslo University Hospital · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RecG is a helicase that is conserved in nearly all bacterial species. The prototypical Escherichia coli RecG promotes regression of stalled replication forks, participates in DNA recombination and DNA repair, and prevents aberrant replication. Mycobacterium tuberculosis RecG (RecGMtb) is a DNA-dependent ATPase that unwinds a variety of DNA substrates, although its preferred substrate is a Holliday junction. Here, we performed site-directed mutagenesis of selected residues in the wedge domain and motifs Q, I, Ib and VI of RecGMtb. Three of the 10 substitution mutations engineered were detected previously as naturally occurring SNPs in the gene encoding RecGMtb. Alanine substitution mutations at residues Q292, F286, K321 and R627 abolished the RecGMtb unwinding activity, whilst RecGMtb F99A, P285S and T408A mutants exhibited ~25-50 % lower unwinding activity than WT. We also found that RecGMtb bound ATP in the absence of a DNA cofactor.

Indexed as

Mutation, MissenseAmino Acid SequenceDNA HelicasesDNA Mutational AnalysisModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedMutant ProteinsMycobacterium tuberculosisProtein ConformationSequence AlignmentDNA HelicasesMutant Proteins

Identifiers

PMID24169816
PMCPMC3917224
OpenAlexW2062059003

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.