Evidence map›Paper›PMID 12024033›Full record

ArticleMolecular and cellular biology2002

Dynamic localization of an Okazaki fragment processing protein suggests a novel role in telomere replication.

Wonchae Choe, Martin Budd, Osamu Imamura, Laura Hoopes, Judith L Campbell

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

44 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
  2. The canonical RPA complex interacts with Est3 to regulate yeast telomerase activity.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. International journal of molecular sciences · 2021
    Review
  8. Review
  9. Article
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  11. Review
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  14. Review
  15. Article
  16. Article
  17. Article
  18. Nuclease activity of Saccharomyces cerevisiae Dna2 inhibits its potent DNA helicase activity.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  19. Article
  20. Four pillars of the S-phase checkpoint.Genes & development · 2013
    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 2 institutions in 2 countries.

Wonchae ChoeBraun Laboratories, Pasadena, California 91125, USA.
Martin Budd
Osamu Imamura
Laura Hoopes
Judith L Campbell
B. Braun (Netherlands) · NLPomona College · US

Funding

ENZYMATIC MECHANISMS OF DNA REPLICATIONR01GM025508 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI CAMPBELL, JUDITH L · 1985 to 2006
$2.5M
NIGMS NIH HHS GM25508NIGMS NIH HHS R01 GM025508
6 · The paper itself

Abstract

We have found that the Dna2 helicase-nuclease, thought to be involved in maturation of Okazaki fragments, is a component of telomeric chromatin. We demonstrate a dynamic localization of Dna2p to telomeres that suggests a dual role for Dna2p, one in telomere replication and another, unknown function, perhaps in telomere capping. Both chromatin immunoprecipitation (ChIP) and immunofluorescence show that Dna2p associates with telomeres but not bulk chromosomal DNA in G(1) phase, when there is no telomere replication and the telomere is transcriptionally silenced. In S phase, there is a dramatic redistribution of Dna2p from telomeres to sites throughout the replicating chromosomes. Dna2p is again localized to telomeres in late S, where it remains through G(2) and until the next S phase. Telomeric localization of Dna2p required Sir3p, since the amount of Dna2p found at telomeres by two different assays, one-hybrid and ChIP, is severely reduced in strains lacking Sir3p. The Dna2p is also distributed throughout the nucleus in cells growing in the presence of double-strand-break-inducing agents such as bleomycin. Finally, we show that Dna2p is functionally required for telomerase-dependent de novo telomere synthesis and also participates in telomere lengthening in mutants lacking telomerase.

Indexed as

Saccharomyces cerevisiae ProteinsSilent Information Regulator Proteins, Saccharomyces cerevisiaeAdenosine TriphosphatasesBase SequenceCell CycleCross-Linking ReagentsDNADNA DamageDNA HelicasesDNA ReplicationFluorescent Antibody Technique, IndirectFungal ProteinsMolecular Sequence DataMutationProtein TransportTelomereAdenosine TriphosphatasesCross-Linking ReagentsDNADNA2 protein, S cerevisiaeDNA HelicasesFungal ProteinsOkazaki fragmentsSaccharomyces cerevisiae ProteinsSilent Information Regulator Proteins, Saccharomyces cerevisiaeSIR3 protein, S cerevisiaeTrans-Activators

Identifiers

PMID12024033
PMCPMC133873
OpenAlexW1969003098

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.