Evidence map›Paper›PMID 23143872›Full record

ArticleProtein & cell2012

Structural insights into the assembly of human translesion polymerase complexes.

Wei Xie, Xuan Yang, Min Xu, Tao Jiang

Open access · bronzeAbstract read
In one paragraph

Article in Protein & cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

25 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Protein-Protein Interactions in Translesion Synthesis.Molecules (Basel, Switzerland) · 2021
    Review
  8. Article
  9. Molecular mechanisms of assembly and TRIP13-mediated remodeling of the human Shieldin complex.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  10. p31Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Article
  12. Review
  13. Article
  14. Mammalian DNA Polymerase Kappa Activity and Specificity.Molecules (Basel, Switzerland) · 2019
    Review
  15. Review
  16. Article
  17. Article
  18. Translesion DNA polymerases in eukaryotes: what makes them tick?Critical reviews in biochemistry and molecular biology · 2017
    Review
  19. Review
  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

4 authors at 2 institutions in 1 country.

Wei XieNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Chaoyang District, Beijing, China.
Xuan Yang
Min Xu
Tao Jiang
Chinese Academy of Sciences · CNInstitute of Biophysics · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In addition to DNA repair pathways, cells utilize translesion DNA synthesis (TLS) to bypass DNA lesions during replication. During TLS, Y-family DNA polymerase (Polη, Polκ, Polı and Rev1) inserts specific nucleotide opposite preferred DNA lesions, and then Polζ consisting of two subunits, Rev3 and Rev7, carries out primer extension. Here, we report the complex structures of Rev3-Rev7-Rev1(CTD) and Rev3-Rev7-Rev1(CTD)-Polκ(RIR). These two structures demonstrate that Rev1(CTD) contains separate binding sites for Polκ and Rev7. Our BIAcore experiments provide additional support for the notion that the interaction between Rev3 and Rev7 increases the affinity of Rev7 and Rev1. We also verified through FRET experiment that Rev1, Rev3, Rev7 and Polκ form a stable quaternary complex in vivo, thereby suggesting an efficient switching mechanism where the "inserter" polymerase can be immediately replaced by an "extender" polymerase within the same quaternary complex.

Indexed as

Binding SitesCrystallography, X-RayDNA-Binding ProteinsDNA-Directed DNA PolymeraseDNA RepairFluorescence Resonance Energy TransferHumansMad2 ProteinsNuclear ProteinsNucleotidyltransferasesProtein BindingProteinsProtein Structure, QuaternaryProtein Structure, TertiaryRecombinant ProteinsY-Family DNA PolymerasesDNA-Binding ProteinsDNA-Directed DNA PolymeraseMAD2L2 protein, humanMad2 ProteinsNuclear ProteinsNucleotidyltransferasesPOLK protein, humanProteinsRecombinant ProteinsREV1 protein, humanREV3L protein, humanY-Family DNA Polymerases

Identifiers

PMID23143872
PMCPMC4875464
OpenAlexW2130892534

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.