Evidence map›Paper›PMID 16963491›Full record

ArticleNucleic acids research2006

A specific loop in human DNA polymerase mu allows switching between creative and DNA-instructed synthesis.

Raquel Juárez, José F Ruiz, Stephanie A Nick McElhinny, Dale Ramsden, Luis Blanco

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

44 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. FromiScience · 2024
    Article
  5. Review
  6. Structural and Molecular Kinetic Features of Activities of DNA Polymerases.International journal of molecular sciences · 2022
    Review
  7. Article
  8. Review
  9. Review
  10. Article
  11. Structure and function relationships in mammalian DNA polymerases.Cellular and molecular life sciences : CMLS · 2020
    Review
  12. Structural evidence for an inThe Journal of biological chemistry · 2019
    Article
  13. Article
  14. Break-induced replication links microsatellite expansion to complex genome rearrangements.BioEssays : news and reviews in molecular, cellular and developmental biology · 2017
    Review
  15. Article
  16. Article
  17. Essential role for polymerase specialization in cellular nonhomologous end joining.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  18. Creative template-dependent synthesis by human polymerase mu.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  19. Article
  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.

Raquel JuárezCentro de Biología Molecular Severo Ochoa (CSIC-UAM), Campus Universidad Autónoma Canto Blanco, 28049 Madrid, Spain.
José F Ruiz
Stephanie A Nick McElhinny
Dale Ramsden
Luis Blanco
University of North Carolina at Chapel Hill · US

Funding

The Role of DNA Synthesis in Nonhomologous End JoiningR01CA097096 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI DALE A RAMSDEN · 2003 to 2026
$5.5M
DNA Polymerases in Nonhomologous End JoiningU01CA097096 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI RAMSDEN, DALE A · 2019 to 2022
$1.4M
NCI NIH HHS CA097096NCI NIH HHS R01 CA097096NCI NIH HHS U01 CA097096
6 · The paper itself

Abstract

Human DNA polymerase mu (Polmu) is a family X member that has terminal transferase activity but, in spite of a non-orthodox selection of the template information, displays its maximal catalytic efficiency in DNA-templated reactions. As terminal deoxynucleotidyl transferase (TdT), Polmu has a specific loop (loop1) that could provide this enzyme with its terminal transferase activity. When loop1 was deleted, human Polmu lacked TdT activity but improved DNA-binding and DNA template-dependent polymerization. Interestingly, when loop1 from TdT was inserted in Polmu (substituting its cognate loop1), the resulting chimaera displayed TdT activity, preferentially inserting dGTP residues, but had a strongly reduced template-dependent polymerization activity. Therefore, a specialized loop in Polmu, that could adopt alternative conformations, appears to provide this enzyme with a dual capacity: (i) template independency to create new DNA information, in which loop1 would have an active role by acting as a 'pseudotemplate'; (ii) template-dependent polymerization, in which loop1 must allow binding of the template strand. Recent in vivo and in vitro data suggest that such a dual capacity could be advantageous to resolve microhomology-mediated end-joining reactions.

Indexed as

Amino Acid SequenceCatalysisDNADNA-Directed DNA PolymeraseDNA NucleotidylexotransferaseDNA, Single-StrandedHumansMolecular Sequence DataProtein BindingProtein Structure, TertiarySequence DeletionTemplates, GeneticDNADNA-Directed DNA PolymeraseDNA NucleotidylexotransferaseDNA polymerase muDNA, Single-Stranded

Identifiers

PMID16963491
PMCPMC1636348
OpenAlexW2110210919

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.