Evidence map›Paper›PMID 18854351›Full record

ArticleNucleic acids research2008

Transcription elongation past O6-methylguanine by human RNA polymerase II and bacteriophage T7 RNA polymerase.

Alexandra Dimitri, John A Burns, Suse Broyde, David A Scicchitano

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.2field-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

23 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  11. Article
  12. Mechanism of RNA polymerase II stalling by DNA alkylation.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  13. Mechanism of DNA alkylation-induced transcriptional stalling, lesion bypass, and mutagenesis.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. Mammalian transcription-coupled excision repair.Cold Spring Harbor perspectives in biology · 2013
    Review
  20. 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 1 institution in 1 country.

Alexandra DimitriDepartment of Biology, New York University, 1009 Silver Center, 100 Washington Square East, New York, NY 10003, USA.
John A Burns
Suse Broyde
David A Scicchitano
New York University · US

Funding

Carcinogen-DNA Adducts: Topology, Conformation and Repair (Renewal)R01CA028038 · NCI · NEW YORK UNIVERSITY · PI BROYDE, SUSE · 1985 to 2014
$4.7M
DNA Lesion Structures: Mutagenicity and RepairR01CA075449 · NCI · NEW YORK UNIVERSITY · PI BROYDE, SUSE · 1997 to 2015
$4.3M
RNA Polymerase Transcription Past DNA AdductsR01ES010581 · NIEHS · NEW YORK UNIVERSITY · PI SCICCHITANO, DAVID A · 2000 to 2013
$3.1M
NCI NIH HHS 2R01 CA75449NCI NIH HHS 5R01 CA28038NIEHS NIH HHS ES010581
6 · The paper itself

Abstract

O(6)-Methylguanine (O(6)-meG) is a major mutagenic, carcinogenic and cytotoxic DNA adduct produced by various endogenous and exogenous methylating agents. We report the results of transcription past a site-specifically modified O(6)-meG DNA template by bacteriophage T7 RNA polymerase and human RNA polymerase II. These data show that O(6)-meG partially blocks T7 RNA polymerase and human RNA polymerase II elongation. In both cases, the sequences of the truncated transcripts indicate that both polymerases stop precisely at the damaged site without nucleotide incorporation opposite the lesion, while extensive misincorporation of uracil is observed in the full-length RNA. For both polymerases, computer models suggest that bypass occurs only when O(6)-meG adopts an anti conformation around its glycosidic bond, with the methyl group in the proximal orientation; in contrast, blockage requires the methyl group to adopt a distal conformation. Furthermore, the selection of cytosine and uracil partners opposite O(6)-meG is rationalized with modeled hydrogen-bonding patterns that agree with experimentally observed O(6)-meG:C and O(6)-meG:U pairing schemes. Thus, in vitro, O(6)-meG contributes substantially to transcriptional mutagenesis. In addition, the partial blockage of RNA polymerase II suggests that transcription-coupled DNA repair could play an auxiliary role in the clearance of this lesion.

Indexed as

Transcription, GeneticDNADNA-Directed RNA PolymerasesGuanineHeLa CellsHumansHydrogen BondingModels, MolecularNucleotidesRNA Polymerase IITemplates, GeneticViral ProteinsYeastsbacteriophage T7 RNA polymeraseDNADNA-Directed RNA PolymerasesGuanineNucleotidesO-(6)-methylguanineRNA Polymerase IIViral Proteins

Identifiers

PMID18854351
PMCPMC2582612
OpenAlexW2051394081

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.