Evidence map›Paper›PMID 30916324›Full record

ArticleNucleic acids research2019

New insights into the structures and interactions of bacterial Y-family DNA polymerases.

Kęstutis Timinskas, Česlovas Venclovas

Abstract read
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing 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

30 citing papers in PubMed.

  1. Article
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  5. Review
  6. Article
  7. Article
  8. The polinton-like supergroup of viruses: evolution, molecular biology, and taxonomy.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  9. Article
  10. Article
  11. Article
  12. Natural history of eukaryotic DNA viruses with double jelly-roll major capsid proteins.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. Jumping DNA polymerases in bacteriophages.bioRxiv : the preprint server for biology · 2024
    Article
  14. Article
  15. Review
  16. Article
  17. Article
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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.

Kęstutis TiminskasInstitute of Biotechnology, Life Sciences Center, Vilnius University, Saulėtekio 7, Vilnius LT-10257, Lithuania.
Česlovas VenclovasInstitute of Biotechnology, Life Sciences Center, Vilnius University, Saulėtekio 7, Vilnius LT-10257, Lithuania.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacterial Y-family DNA polymerases are usually classified into DinB (Pol IV), UmuC (the catalytic subunit of Pol V) and ImuB, a catalytically dead essential component of the ImuA-ImuB-DnaE2 mutasome. However, the true diversity of Y-family polymerases is unknown. Furthermore, for most of them the structures are unavailable and interactions are poorly characterized. To gain a better understanding of bacterial Y-family DNA polymerases, we performed a detailed computational study. It revealed substantial diversity, far exceeding traditional classification. We found that a large number of subfamilies feature a C-terminal extension next to the common Y-family region. Unexpectedly, in most C-terminal extensions we identified a region homologous to the N-terminal oligomerization motif of RecA. This finding implies a universal mode of interaction between Y-family members and RecA (or ImuA), in the case of Pol V strongly supported by experimental data. In gram-positive bacteria, we identified a putative Pol V counterpart composed of a Y-family polymerase, a YolD homolog and RecA. We also found ImuA-ImuB-DnaE2 variants lacking ImuA, but retaining active or inactive Y-family polymerase, a standalone ImuB C-terminal domain and/or DnaE2. In summary, our analyses revealed that, despite considerable diversity, bacterial Y-family polymerases share previously unanticipated similarities in their structural domains/motifs and interactions.

Indexed as

Protein ConformationAmino Acid SequenceCatalytic DomainComputational BiologyCytoskeletonDNA-Binding ProteinsDNA-Directed DNA PolymeraseDNA Polymerase IIIEscherichia coliEscherichia coli ProteinsModels, MolecularRec A RecombinasesDinB protein, E coliDNA-Binding ProteinsDNA-Directed DNA PolymeraseDNA Polymerase IIIDNA polymerase III, alpha subunitEscherichia coli ProteinsrecA protein, E coliRec A RecombinasesUmuC protein, E coli

Identifiers

PMID30916324
PMCPMC6511836

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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.