Evidence map›Paper›PMID 20671026›Full record

ArticleNucleic acids research2010

Arrest of human mitochondrial RNA polymerase transcription by the biological aldehyde adduct of DNA, M1dG.

Susan D Cline, M Fernanda Lodeiro, Lawrence J Marnett, Craig E Cameron, Jamie J Arnold

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2010. 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
0.9field-weighted citation impact, top 25% 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, 24 citations in OpenAlex.

  1. Article
  2. Mitochondrial DNA damage as driver of cellular outcomes.American journal of physiology. Cell physiology · 2022
    Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Mitochondrial DNA damage induced autophagy, cell death, and disease.Frontiers in bioscience (Landmark edition) · 2016
    Review
  9. Article
  10. Review
  11. Mitochondria as a target of environmental toxicants.Toxicological sciences : an official journal of the Society of Toxicology · 2013
    Review
  12. Article
  13. Article
  14. Review
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

5 authors at 2 institutions in 1 country.

Susan D ClineDivision of Basic Medical Sciences, Mercer University School of Medicine, Mercer, GA 31207, USA. cline_sd@mercer.edu
M Fernanda Lodeiro
Lawrence J Marnett
Craig E Cameron
Jamie J Arnold
Mercer University · USVanderbilt University · US

Funding

Chemistry and Biology of Malondialdehyde DNA AdductsR37CA087819 · NCI · VANDERBILT UNIVERSITY · PI MARNETT, LAWRENCE J. · 2005 to 2014
$4.2M
CHEMISTRY AND BIOLOGY OF MALONDIALDEHYDE DNA ADDUCTSR01CA087819 · NCI · VANDERBILT UNIVERSITY · PI MARNETT, LAWRENCE J. · 2000 to 2020
$4.0M
Reactive Aldehyde DNA Damage in Mitochondrial Mutagenesis and Disease PathophysioR15GM087681 · NIGMS · MERCER UNIVERSITY MACON · PI CLINE, SUSAN D. · 2009 to 2009
$227k
NCI NIH HHS CA087819NIGMS NIH HHS GM087681NIGMS NIH HHS R15 GM087681
6 · The paper itself

Abstract

The biological aldehydes, malondialdehyde and base propenal, react with DNA to form a prevalent guanine adduct, M(1)dG. The exocyclic ring of M(1)dG opens to the acyclic N(2)-OPdG structure when paired with C but remains closed in single-stranded DNA or when mispaired with T. M(1)dG is a target of nucleotide excision repair (NER); however, NER is absent in mitochondria. An in vitro transcription system with purified human mitochondrial RNA polymerase (POLRMT) and transcription factors, mtTFA and mtTFB2, was used to determine the effect of M(1)dG on POLRMT elongation. DNA templates contained a single adduct opposite either C or T downstream of either the light-strand (LSP) or heavy-strand (HSP1) promoter for POLRMT. M(1)dG in the transcribed strand arrested 60-90% POLRMT elongation complexes with greater arrest by the adduct when opposite T. POLRMT was more sensitive to N(2)-OPdG and M(1)dG after initiation at LSP, which suggests promoter-specific differences in the function of POLRMT complexes. A closed-ring analog of M(1)dG, PdG, blocked ≥95% of transcripts originating from either promoter regardless of base pairing, and the transcripts remained associated with POLRMT complexes after stalling at the adduct. This work suggests that persistent M(1)dG adducts in mitochondrial DNA hinder the transcription of mitochondrial genes.

Indexed as

Transcription, GeneticDeoxyguanosineDNA AdductsDNA-Directed RNA PolymerasesHumansMitochondriaPromoter Regions, GeneticPurine Nucleosides1,N2-propano-2'-deoxyguanosine3-(2'-deoxy-beta-D-erythro-pentofuranosyl)pyrimido(1,2-alpha)purin-10(3H)-oneDeoxyguanosineDNA AdductsDNA-Directed RNA PolymerasesPOLRMT protein, humanPurine Nucleosides

Identifiers

PMID20671026
PMCPMC2995074
OpenAlexW2148040481

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.