Evidence map›Paper›PMID 25646444›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Archaeal replicative primases can perform translesion DNA synthesis.

Stanislaw K Jozwiakowski, Farimah Borazjani Gholami, Aidan J Doherty

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

24 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. DNA polymerase α-primase can function as a translesion DNA polymerase.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Archaeal DNA Replication.Annual review of microbiology · 2020
    Review
  9. Genetic Control of Oxidative Mutagenesis inJournal of bacteriology · 2020
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  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

3 authors at 1 institution in 1 country.

Stanislaw K JozwiakowskiGenome Damage and Stability Centre, School of Life Sciences, University of Sussex, Brighton BN1 9RQ, United Kingdom.
Farimah Borazjani GholamiGenome Damage and Stability Centre, School of Life Sciences, University of Sussex, Brighton BN1 9RQ, United Kingdom.
Aidan J DohertyGenome Damage and Stability Centre, School of Life Sciences, University of Sussex, Brighton BN1 9RQ, United Kingdom ajd21@sussex.ac.uk.
University of Sussex · GB

Funding

Biotechnology and Biological Sciences Research Council BB/H019723/1Biotechnology and Biological Sciences Research Council BB/J018643/1Medical Research Council G080130
6 · The paper itself

Abstract

DNA replicases routinely stall at lesions encountered on the template strand, and translesion DNA synthesis (TLS) is used to rescue progression of stalled replisomes. This process requires specialized polymerases that perform translesion DNA synthesis. Although prokaryotes and eukaryotes possess canonical TLS polymerases (Y-family Pols) capable of traversing blocking DNA lesions, most archaea lack these enzymes. Here, we report that archaeal replicative primases (Pri S, primase small subunit) can also perform TLS. Archaeal Pri S can bypass common oxidative DNA lesions, such as 8-Oxo-2'-deoxyguanosines and UV light-induced DNA damage, faithfully bypassing cyclobutane pyrimidine dimers. Although it is well documented that archaeal replicases specifically arrest at deoxyuracils (dUs) due to recognition and binding to the lesions, a replication restart mechanism has not been identified. Here, we report that Pri S efficiently replicates past dUs, even in the presence of stalled replicase complexes, thus providing a mechanism for maintaining replication bypass of these DNA lesions. Together, these findings establish that some replicative primases, previously considered to be solely involved in priming replication, are also TLS proficient and therefore may play important roles in damage tolerance at replication forks.

Indexed as

DNA DamageArchaeaBiocatalysisDNA, ArchaealDNA PrimaseOxidative StressDNA, ArchaealDNA PrimaseAEParchaeaprimasereplicationtranslesion synthesis

Identifiers

PMID25646444
PMCPMC4343091
OpenAlexW2112207222

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.