Evidence map›Paper›PMID 15302919›Full record

ArticleNucleic acids research2004

Genetic and biochemical analyses of Pfh1 DNA helicase function in fission yeast.

Gi-Hyuck Ryu, Hiroyuki Tanaka, Do-Hyung Kim, Jeong-Hoon Kim, Sung-Ho Bae, Young-Nam Kwon, Joon Shick Rhee, Stuart A MacNeill, Yeon-Soo Seo

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
1.0field-weighted citation impact, top 28% 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

46 citing papers in PubMed, 54 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. Role and Regulation of Pif1 Family Helicases at the Replication Fork.International journal of molecular sciences · 2022
    Review
  4. International journal of molecular sciences · 2021
    Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. 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
  10. Review
  11. TheGenetics · 2019
    Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Pif1 is a force-regulated helicase.Nucleic acids research · 2016
    Article
  19. Article
  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

9 authors at 1 institution in 1 country.

Gi-Hyuck RyuNational Creative Research Initiative Center for Cell Cycle Control, Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon, 305-701, Korea.
Hiroyuki Tanaka
Do-Hyung Kim
Jeong-Hoon Kim
Sung-Ho Bae
Young-Nam Kwon
Joon Shick Rhee
Stuart A MacNeill
Yeon-Soo Seo
Creative Research · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Schizosaccharomyces pombe pfh1+ gene (PIF1 homolog) encodes an essential enzyme that has both DNA helicase and ATPase activities and is implicated in lagging strand DNA processing. Mutations in the pfh1+ gene suppress a temperature-sensitive allele of cdc24+, which encodes a protein that functions with Schizosaccharomyces pombe Dna2 in Okazaki fragment processing. In this study, we describe the enzymatic properties of the Pfh1 helicase and the genetic interactions between pfh1 and cdc24, dna2, cdc27 or pol 3, all of which are involved in the Okazaki fragment metabolism. We show that a full-length Pfh1 fusion protein is active as a monomer. The helicase activity of Pfh1 displaced only short (<30 bp) duplex DNA regions efficiently in a highly distributive manner and was markedly stimulated by the presence of a replication-fork-like structure in the substrate. The temperature-sensitive phenotype of a dna2-C2 or a cdc24-M38 mutant was suppressed by pfh1-R20 (a cold-sensitive mutant allele of pfh1) and overexpression of wild-type pfh1+ abolished the ability of the pfh1 mutant alleles to suppress dna2-C2 and cdc24-M38. Purified Pfh1-R20 mutant protein displayed significantly reduced ATPase and helicase activities. These results indicate that the simultaneous loss-of-function mutations of pfh1+ and dna2+ (or cdc24+) are essential to restore the growth defect. Our genetic data indicate that the Pfh1 DNA helicase acts in concert with Cdc24 and Dna2 to process single-stranded DNA flaps generated in vivo by pol -mediated lagging strand displacement DNA synthesis.

Indexed as

Adenosine TriphosphatasesCell Cycle ProteinsCell DivisionDNADNA HelicasesEscherichia coli ProteinsGenes, FungalMutationNucleic Acid ConformationPeptide Elongation FactorsSchizosaccharomycesSchizosaccharomyces pombe ProteinsSubstrate SpecificitySuppression, GeneticTemplates, GeneticTranscriptional Elongation FactorsAdenosine TriphosphatasesCdc24 protein, S pombeCell Cycle ProteinsDNADNA HelicasesEscherichia coli ProteinsnusA protein, E coliOkazaki fragmentsPeptide Elongation FactorsPfh1 protein, S pombeSchizosaccharomyces pombe ProteinsTranscriptional Elongation FactorsTranscription Factors

Identifiers

PMID15302919
PMCPMC514361
OpenAlexW2040167235

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.