Evidence map›Paper›PMID 22918593›Full record

ReviewSub-cellular biochemistry2012

DNA ligase I, the replicative DNA ligase.

Timothy R L Howes, Alan E Tomkinson

Abstract readReview
In one paragraph

Review in Sub-cellular biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

40 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
  2. Article
  3. mSphere · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
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  13. Article
  14. Review
  15. Review
  16. Article
  17. DNA Mismatch Repair and its Role in Huntington's Disease.Journal of Huntington's disease · 2021
    Review
  18. Article
  19. Article
  20. Review
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.

Timothy R L HowesBiomedical Sciences Graduate Program, University of New Mexico, Cancer Research Facility MSC08 4640, 1 University of New Mexico, Albuquerque, NM, 87131-0001, USA, howes.timothy@gmail.com.
Alan E Tomkinson
University of New Mexico · US

Funding

Transcription-Coupled & Replication-Associated Excision RepairP01CA092584 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI John A. Tainer · 2001 to 2026
$89.6M
ROLES OF DNA LIGASE I IN MAMMALIAN DNA METABOLISMR01GM057479 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR SAN ANT · PI TOMKINSON, ALAN E · 2000 to 2017
$3.7M
NCI NIH HHS P01 CA092584NIGMS NIH HHS R01 GM057479
6 · The paper itself

Abstract

Multiple DNA ligation events are required to join the Okazaki fragments generated during lagging strand DNA synthesis. In eukaryotes, this is primarily carried out by members of the DNA ligase I family. The C-terminal catalytic region of these enzymes is composed of three domains: a DNA binding domain, an adenylation domain and an OB-fold domain. In the absence of DNA, these domains adopt an extended structure but transition into a compact ring structure when they engage a DNA nick, with each of the domains contacting the DNA. The non-catalytic N-terminal region of eukaryotic DNA ligase I is responsible for the specific participation of these enzymes in DNA replication. This proline-rich unstructured region contains the nuclear localization signal and a PCNA interaction motif that is critical for localization to replication foci and efficient joining of Okazaki fragments. DNA ligase I initially engages the PCNA trimer via this interaction motif which is located at the extreme N-terminus of this flexible region. It is likely that this facilitates an additional interaction between the DNA binding domain and the PCNA ring. The similar size and shape of the rings formed by the PCNA trimer and the DNA ligase I catalytic region when it engages a DNA nick suggest that these proteins interact to form a double-ring structure during the joining of Okazaki fragments. DNA ligase I also interacts with replication factor C, the factor that loads the PCNA trimeric ring onto DNA. This interaction, which is regulated by phosphorylation of the non-catalytic N-terminus of DNA ligase I, also appears to be critical for DNA replication.

Indexed as

DNA Breaks, Single-StrandedAmino Acid MotifsAnimalsDNADNA Ligase ATPDNA LigasesDNA ReplicationHumansNuclear Localization SignalsProliferating Cell Nuclear AntigenProtein Structure, QuaternaryProtein Structure, TertiaryReplication Protein CDNADNA Ligase ATPDNA LigasesLIG1 protein, humanNuclear Localization SignalsOkazaki fragmentsProliferating Cell Nuclear AntigenReplication Protein C

Identifiers

PMID22918593
PMCPMC3881551
OpenAlexW154360567

What OpenQuestion holds

Textmetadata
LicenceTDM
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.