Evidence map›Paper›PMID 20212037›Full record

ArticleThe Journal of biological chemistry2010

Structural basis of O6-alkylguanine recognition by a bacterial alkyltransferase-like DNA repair protein.

James M Aramini, Julie L Tubbs, Sreenivas Kanugula, Paolo Rossi, Asli Ertekin, Melissa Maglaqui, Keith Hamilton, Colleen T Ciccosanti, Mei Jiang, Rong Xiao and 7 more

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 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.8field-weighted citation impact, top 16% 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, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Alkyltransferase-like protein clusters scan DNA rapidly over long distances and recruit NER to alkyl-DNA lesions.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Review
  9. Article
  10. DNA repair by reversal of DNA damage.Cold Spring Harbor perspectives in biology · 2013
    Review
  11. Review
  12. Alkyltransferase-like protein (Atl1) distinguishes alkylated guanines for DNA repair using cation-π interactions.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  13. Article
  14. Article
  15. Review
  16. 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

17 authors at 6 institutions in 1 country.

James M AraminiCenter for Advanced Biotechnology and Medicine, Department of Molecular Biology and Biochemistry, Rutgers, The State University of New Jersey, Piscataway, New Jersey 08854, USA. jma@cabm.rutgers.edu
Julie L Tubbs
Sreenivas Kanugula
Paolo Rossi
Asli Ertekin
Melissa Maglaqui
Keith Hamilton
Colleen T Ciccosanti
Mei Jiang
Rong Xiao
Ta-Tsen Soong
Burkhard Rost
Thomas B Acton
John K Everett
Anthony E Pegg
John A Tainer
Gaetano T Montelione
Advanced Pharma · USRutgers, The State University of New Jersey · USPennsylvania State University · USScripps Research Institute · USColumbia University · USNew York Structural Biology Center · US

Funding

Sub-project 9U54GM074958 · NIGMS · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI MONTELIONE, GAETANO T · 2005 to 2009
$56.6M
Structural Biochemistry of DNA DealkylationR01CA097209 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI TAINER, JOHN A. · 2002 to 2014
$4.4M
PERSISTENCE OF ALKYLATED DNA IN CARCINOGENESISR01CA018137 · NCI · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI KANUGULA, SREENIVAS · 1985 to 2011
$2.8M
PERSISTENCE OF ALKYLATED DNA IN CARCINOGENESISR37CA018137 · NCI · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI PEGG, ANTHONY E · 1989 to 2009
$972k
NCI NIH HHS CA018137NCI NIH HHS CA097209NCI NIH HHS R01 CA018137NCI NIH HHS R01 CA097209NCI NIH HHS R37 CA018137NIGMS NIH HHS U54 GM074958NIGMS NIH HHS U54-GM074958
6 · The paper itself

Abstract

Alkyltransferase-like proteins (ATLs) are a novel class of DNA repair proteins related to O(6)-alkylguanine-DNA alkyltransferases (AGTs) that tightly bind alkylated DNA and shunt the damaged DNA into the nucleotide excision repair pathway. Here, we present the first structure of a bacterial ATL, from Vibrio parahaemolyticus (vpAtl). We demonstrate that vpAtl adopts an AGT-like fold and that the protein is capable of tightly binding to O(6)-methylguanine-containing DNA and disrupting its repair by human AGT, a hallmark of ATLs. Mutation of highly conserved residues Tyr(23) and Arg(37) demonstrate their critical roles in a conserved mechanism of ATL binding to alkylated DNA. NMR relaxation data reveal a role for conformational plasticity in the guanine-lesion recognition cavity. Our results provide further evidence for the conserved role of ATLs in this primordial mechanism of DNA repair.

Indexed as

Protein FoldingAlkyl and Aryl TransferasesAmino Acid SubstitutionDNADNA RepairGuanineHumansMutation, MissenseVibrio parahaemolyticusAlkyl and Aryl TransferasesDNAGuanineO-(6)-methylguanine

Identifiers

PMID20212037
PMCPMC2859536
OpenAlexW2127087714

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.