Evidence map›Paper›PMID 10217775›Full record

ArticleJournal of bacteriology1999

Purification and characterization of Thermotoga maritima endonuclease IV, a thermostable apurinic/apyrimidinic endonuclease and 3'-repair diesterase.

B J Haas, M Sandigursky, J A Tainer, W A Franklin, R P Cunningham

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 1999. 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
0.8field-weighted citation impact, top 28% 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, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. The Complete Genome Sequence of HyperthermophileFrontiers in microbiology · 2016
    Article
  7. Article
  8. Article
  9. DNA sequence context conceals α-anomeric lesions.Journal of molecular biology · 2012
    Article
  10. Structure of the endonuclease IV homologue from Thermotoga maritima in the presence of active-site divalent metal ions.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010
    Article
  11. Purification, crystallization and preliminary crystallographic analysis of a thermostable endonuclease IV from Thermotoga maritima.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009
    Article
  12. Article
  13. Article
  14. 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

5 authors at 3 institutions in 1 country.

B J HaasDepartment of Biological Sciences, State University of New York at Albany, Albany, New York 12222, USA.
M Sandigursky
J A Tainer
W A Franklin
R P Cunningham
Albert Einstein College of Medicine · USUniversity at Albany, State University of New York · USScripps Research Institute · US

Funding

STRUCTURE AND FUNCTION OF METALLOENZYMES FOR DNA REPAIRR01GM046312 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI TAINER, JOHN A. · 1991 to 2012
$5.9M
NOVEL ENZYME ACTING ON OXIDATIVE DNA DAMAGER01CA052025 · NCI · YESHIVA UNIVERSITY · PI FRANKLIN, WILLIAM A · 1996 to 2000
$250k
NOVEL ENZYME ACTING ON RADIATION-DAMAGED DNAR29CA052025 · NCI · YESHIVA UNIVERSITY · PI FRANKLIN, WILLIAM A · 1990 to 1994
–
NCI NIH HHS CA52025NIGMS NIH HHS GM46312NIGMS NIH HHS R01 GM046312
6 · The paper itself

Abstract

An endonuclease IV homolog was identified as the product of a conceptual open reading frame in the genome of the hyperthermophilic bacterium Thermotoga maritima. The T. maritima endonuclease IV gene encodes a 287-amino-acid protein with 32% sequence identity to Escherichia coli endonuclease IV. The gene was cloned, and the expressed protein was purified and shown to have enzymatic activities that are characteristic of the endonuclease IV family of DNA repair enzymes, including apurinic/apyrimidinic endonuclease activity and repair activities on 3'-phosphates, 3'-phosphoglycolates, and 3'-trans-4-hydroxy-2-pentenal-5-phosphates. The T. maritima enzyme exhibits enzyme activity at both low and high temperatures. Circular dichroism spectroscopy indicates that T. maritima endonuclease IV has secondary structure similar to that of E. coli endonuclease IV and that the T. maritima endonuclease IV structure is more stable than E. coli endonuclease IV by almost 20 degrees C, beginning to rapidly denature only at temperatures approaching 90 degrees C. The presence of this enzyme, which is part of the DNA base excision repair pathway, suggests that thermophiles use a mechanism similar to that used by mesophiles to deal with the large number of abasic sites that arise in their chromosomes due to the increased rates of DNA damage at elevated temperatures.

Indexed as

Escherichia coli ProteinsAmino Acid SequenceCarbon-Oxygen LyasesCloning, MolecularDeoxyribonuclease IV (Phage T4-Induced)DNA-(Apurinic or Apyrimidinic Site) LyaseDNA RepairEnzyme StabilityGenes, BacterialHot TemperatureMolecular Sequence DataRecombinant ProteinsSequence Homology, Amino AcidThermotoga maritimaCarbon-Oxygen LyasesDeoxyribonuclease IV (Phage T4-Induced)DNA-(Apurinic or Apyrimidinic Site) Lyaseendonuclease IV, E coliEscherichia coli ProteinsRecombinant Proteins

Identifiers

PMID10217775
PMCPMC93726
OpenAlexW2157258265

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.