Evidence map›Paper›PMID 23245850›Full record

ArticleStructure (London, England : 1993)2013

Y-family polymerase conformation is a major determinant of fidelity and translesion specificity.

Ryan C Wilson, Meghan A Jackson, Janice D Pata

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
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

20 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Structural and Molecular Kinetic Features of Activities of DNA Polymerases.International journal of molecular sciences · 2022
    Review
  7. Mechanism Underlying the Bypass of Apurinic/Pyrimidinic Site Analogs byInternational journal of molecular sciences · 2022
    Article
  8. Review
  9. Article
  10. Mammalian DNA Polymerase Kappa Activity and Specificity.Molecules (Basel, Switzerland) · 2019
    Review
  11. Article
  12. Article
  13. Translesion DNA polymerases in eukaryotes: what makes them tick?Critical reviews in biochemistry and molecular biology · 2017
    Review
  14. Article
  15. Review
  16. Review
  17. Article
  18. 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

3 authors.

Ryan C WilsonWadsworth Center, New York State Department of Health, Albany, NY 12201-0509, USA.
Meghan A JacksonWadsworth Center, New York State Department of Health, Albany, NY 12201-0509, USA.
Janice D PataWadsworth Center, New York State Department of Health, Albany, NY 12201-0509, USA; Department of Biomedical Sciences, University at Albany, Albany, NY 12201-0509, USA. Electronic address: jpata@wadsworth.org.

Funding

Structural and Mechanistic Studies of Error-Prone PolymerasesR01GM080573 · NIGMS · WADSWORTH CENTER · PI PATA, JANICE D · 2008 to 2018
$2.6M
NIGMS NIH HHS R01 GM080573NIGMS NIH HHS R01-GM080573
6 · The paper itself

Abstract

Y-family polymerases help cells tolerate DNA damage by performing translesion synthesis opposite damaged DNA bases, yet they also have a high intrinsic error rate. We constructed chimeras of two closely related Y-family polymerases that display distinctly different activity profiles and found that the polypeptide linker that tethers the catalytic polymerase domain to the C-terminal DNA-binding domain is a major determinant of overall polymerase activity, nucleotide incorporation fidelity, and abasic site-bypass ability. Exchanging just 3 out of the 15 linker residues is sufficient to interconvert the polymerase activities tested. Crystal structures of four chimeras show that the conformation of the protein correlates with the identity of the interdomain linker sequence. Thus, residues that are more than 15 Å away from the active site are able to influence many aspects of polymerase activity by altering the relative orientations of the catalytic and DNA-binding domains.

Indexed as

Amino Acid SequenceApurinic AcidArchaeal ProteinsBase SequenceCatalytic DomainCrystallography, X-RayDNA Polymerase betaDNA RepairModels, MolecularMolecular Sequence DataNucleic Acid ConformationProtein BindingProtein Structure, SecondaryRecombinant Fusion ProteinsSubstrate SpecificitySulfolobus acidocaldariusApurinic AcidArchaeal ProteinsDNA Polymerase betaRecombinant Fusion Proteins

Identifiers

PMID23245850
PMCPMC3545038

What OpenQuestion holds

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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.