Evidence map›Paper›PMID 12930960›Full record

ArticleNucleic acids research2003

Analysis of the DNA joining repertoire of Chlorella virus DNA ligase and a new crystal structure of the ligase-adenylate intermediate.

Mark Odell, Lucy Malinina, Verl Sriskanda, Marianna Teplova, Stewart Shuman

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
5.0field-weighted citation impact, top 5% 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

21 citing papers in PubMed, 37 citations in OpenAlex.

  1. Fidelity of DNA ligase I is sensitive to physiological MgThe Journal of biological chemistry · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. 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
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. The Phycodnaviridae: the story of how tiny giants rule the world.Current topics in microbiology and immunology · 2009
    Review
  17. The associative nature of adenylyl transfer catalyzed by T4 DNA ligase.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  18. Dynamics of phosphodiester synthesis by DNA ligase.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  19. 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

5 authors at 1 institution in 1 country.

Mark OdellSloan-Kettering Institute, New York, NY 10021, USA.
Lucy Malinina
Verl Sriskanda
Marianna Teplova
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
DNA COMPLEXES--ANTITUMOR DRUGS AND CHEMOTHERAPYR01CA046778 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI PATEL, DINSHAW J · 1988 to 2002
$832k
NCI NIH HHS CA46778NIGMS NIH HHS GM63611NIGMS NIH HHS R01 GM063611
6 · The paper itself

Abstract

Chlorella virus DNA ligase is the smallest eukaryotic ATP-dependent DNA ligase known; it suffices for yeast cell growth in lieu of the essential yeast DNA ligase Cdc9. The Chlorella virus ligase-adenylate intermediate has an intrinsic nick sensing function and its DNA footprint extends 8-9 nt on the 3'-hydroxyl (3'-OH) side of the nick and 11-12 nt on the 5'-phosphate (5'-PO4) side. Here we establish the minimal length requirements for ligatable 3'-OH and 5'-PO4 strands at the nick (6 nt) and describe a new crystal structure of the ligase-adenylate in a state construed to reflect the configuration of the active site prior to nick recognition. Comparison with a previous structure of the ligase-adenylate bound to sulfate (a mimetic of the nick 5'-PO4) suggests how the positions and contacts of the active site components and the bound adenylate are remodeled by DNA binding. We find that the minimal Chlorella virus ligase is capable of catalyzing non-homologous end-joining reactions in vivo in yeast, a process normally executed by the structurally more complex cellular Lig4 enzyme. Our results suggest a model of ligase evolution in which: (i) a small 'pluripotent' ligase is the progenitor of the much larger ligases found presently in eukaryotic cells and (ii) gene duplications, variations within the core ligase structure and the fusion of new domains to the core structure (affording new protein-protein interactions) led to the compartmentalization of eukaryotic ligase function, i.e. by enhancing some components of the functional repertoire of the ancestral ligase while disabling others.

Indexed as

Viral ProteinsAdenosine MonophosphateBase SequenceBinding SitesCatalysisCrystallography, X-RayDNADNA LigasesDNA RepairPhosphatesPlasmidsProtein FoldingProtein Structure, SecondaryProtein Structure, TertiaryAdenosine MonophosphateChlorella virus DNA ligaseDNADNA LigasesPhosphatesViral Proteins

Identifiers

PMID12930960
PMCPMC212790
OpenAlexW2013855018

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.