Evidence map›Paper›PMID 16199559›Full record

ArticleJournal of bacteriology2005

Characterization of a thermophilic ATP-dependent DNA ligase from the euryarchaeon Pyrococcus horikoshii.

Niroshika Keppetipola, Stewart Shuman

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.3field-weighted citation impact, top 23% 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

16 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. ATP-dependent DNA ligase from Thermococcus sp. 1519 displays a new arrangement of the OB-fold domain.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012
    Article
  8. Article
  9. Article
  10. Article
  11. DNA ligases: progress and prospects.The Journal of biological chemistry · 2009
    Review
  12. Overexpression, purification and crystallization of a thermostable DNA ligase from the archaeon Thermococcus sp. 1519.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009
    Article
  13. A purple acidophilic di-ferric DNA ligase from Ferroplasma.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  14. Article
  15. Article
  16. 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

2 authors at 1 institution in 1 country.

Niroshika KeppetipolaMolecular Biology Program, Sloan-Kettering Institute, New York, NY 10021, USA.
Stewart Shuman
Kettering University · US

Funding

Viral DNA and RNA LigasesR01GM063611 · NIGMS · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI SHUMAN, STEWART H · 2001 to 2017
$5.4M
NIGMS NIH HHS GM63611NIGMS NIH HHS R01 GM063611
6 · The paper itself

Abstract

Archaea encode a DNA ligase composed of a C-terminal catalytic domain typical of ATP-dependent ligases plus an N-terminal domain similar to that found in eukaryotic cellular and poxvirus DNA ligases. All archaeal DNA ligases characterized to date have ATP-dependent adenylyltransferase and nick-joining activities. However, recent reports of dual-specificity ATP/NAD+ ligases in two Thermococcus species and Pyrococcus abyssi and an ATP/ADP ligase in Aeropyrum pernix raise the prospect that certain archaeal enzymes might exemplify an undifferentiated ancestral stage in the evolution of ligase substrate specificity. Here we analyze the biochemical properties of Pyrococcus horikoshii DNA ligase. P. horikoshii ligase catalyzes auto-adenylylation and nick sealing in the presence of a divalent cation and ATP; it is unable to utilize NAD+ or ADP to promote ligation in lieu of ATP. P. horikoshii ligase is thermophilic in vitro, with optimal adenylyltransferase activity at 90 degrees C and nick-joining activity at 70 to 90 degrees C. P. horikoshii ligase resembles the ligases of Methanobacterium thermautotrophicum and Sulfolobus shibatae in its strict specificity for ATP.

Indexed as

Adenosine DiphosphateAdenosine MonophosphateAdenosine TriphosphateArchaeal ProteinsBase SequenceDNA, ArchaealDNA LigasesNucleic Acid ConformationNucleotidyltransferasesPyrococcus horikoshiiSubstrate SpecificityAdenosine DiphosphateAdenosine MonophosphateAdenosine TriphosphateArchaeal ProteinsDNA, ArchaealDNA LigasesNucleotidyltransferases

Identifiers

PMID16199559
PMCPMC1251619
OpenAlexW1996696481

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.