Evidence map›Paper›PMID 27001517›Full record

ArticleNucleic acids research2016

Pif1 removes a Rap1-dependent barrier to the strand displacement activity of DNA polymerase δ.

Katrina N Koc, Saurabh P Singh, Joseph L Stodola, Peter M Burgers, Roberto Galletto

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

29 citing papers in PubMed, 38 citations in OpenAlex.

  1. Regulation of Pfh1 helicase activity by nucleic acid interactions and mitochondrial SSB.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Article
  4. Interstitial telomeric sequences promote gross chromosomal rearrangement via multiple mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Role and Regulation of Pif1 Family Helicases at the Replication Fork.International journal of molecular sciences · 2022
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Branched unwinding mechanism of the Pif1 family of DNA helicases.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  17. Review
  18. TheGenetics · 2019
    Article
  19. Genetics · 2019
    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.

Katrina N KocDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, Saint Louis, MO 63110, USA.
Saurabh P SinghDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, Saint Louis, MO 63110, USA.
Joseph L StodolaDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, Saint Louis, MO 63110, USA.
Peter M BurgersDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, Saint Louis, MO 63110, USA.
Roberto GallettoDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, Saint Louis, MO 63110, USA galletto@biochem.wustl.edu.
Washington University in St. Louis · US

Funding

ENZYMOLOGY OF REPLICATION OF YEAST CHROMOSOMAL DNAR01GM032431 · NIGMS · WASHINGTON UNIVERSITY · PI BURGERS, PETER M · 1985 to 2015
$6.5M
HELICASE ACTIVITY AND ITS ROLE IN TELOMERE AND TELOMERASE REGULATIONR01GM098509 · NIGMS · WASHINGTON UNIVERSITY · PI GALLETTO, ROBERTO · 2011 to 2020
$2.7M
NIGMS NIH HHS R01 GM032431NIGMS NIH HHS R01 GM098509
6 · The paper itself

Abstract

Using an in vitro reconstituted system in this work we provide direct evidence that the yeast repressor/activator protein 1 (Rap1), tightly bound to its consensus site, forms a strong non-polar barrier for the strand displacement activity of DNA polymerase δ. We propose that relief of inhibition may be mediated by the activity of an accessory helicase. To this end, we show that Pif1, a 5'-3' helicase, not only stimulates the strand displacement activity of Pol δ but it also allows efficient replication through the block, by removing bound Rap1 in front of the polymerase. This stimulatory activity of Pif1 is not limited to the displacement of a single Rap1 molecule; Pif1 also allows Pol δ to carry out DNA synthesis across an array of bound Rap1 molecules that mimics a telomeric DNA-protein assembly. This activity of Pif1 represents a novel function of this helicase during DNA replication.

Indexed as

DNA ReplicationDNADNA HelicasesDNA Polymerase IIISaccharomyces cerevisiae ProteinsShelterin ComplexTelomere-Binding ProteinsTranscription FactorsDNADNA2 protein, S cerevisiaeDNA HelicasesDNA Polymerase IIIPIF1 protein, S cerevisiaeRAP1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsShelterin ComplexTelomere-Binding ProteinsTranscription Factors

Identifiers

PMID27001517
PMCPMC4856994
OpenAlexW2312944452

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.