Evidence map›Paper›PMID 18851837›Full record

ArticleMolecular cell2008

Mrc1 and DNA polymerase epsilon function together in linking DNA replication and the S phase checkpoint.

Huiqiang Lou, Makiko Komata, Yuki Katou, Zhiyun Guan, Clara C Reis, Martin Budd, Katsuhiko Shirahige, Judith L Campbell

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 134 papers.

0numbers the graph read from it
0cells of the map it votes in
134citing papers in PubMed
7.0field-weighted citation impact, top 2% 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

134 citing papers in PubMed, 206 citations in OpenAlex.

  1. Article
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  13. Revised mechanism of hydroxyurea-induced cell cycle arrest and an improved alternative.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  14. Article
  15. Review
  16. The TIMELESS effort for timely DNA replication and protection.Cellular and molecular life sciences : CMLS · 2023
    Review
  17. Article
  18. Rad53 arrests leading and lagging strand DNA synthesis via distinct mechanisms in response to DNA replication stress.BioEssays : news and reviews in molecular, cellular and developmental biology · 2022
    Article
  19. Article
  20. Article

74 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 2 countries.

Huiqiang LouBraun Laboratories, California Institute of Technology, Pasadena, CA 91125, USA.
Makiko Komata
Yuki Katou
Zhiyun Guan
Clara C Reis
Martin Budd
Katsuhiko Shirahige
Judith L Campbell
California Institute of Technology · USTokyo Institute of Technology · JP

Funding

ENZYMATIC MECHANISMS OF DNA REPLICATIONR01GM025508 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI CAMPBELL, JUDITH L · 1985 to 2006
$2.5M
Enzyme Interactions at the DNA Replication ForkR01GM078666 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI CAMPBELL, JUDITH L · 2006 to 2009
$1.5M
NIGMS NIH HHS GM087666NIGMS NIH HHS GM25508NIGMS NIH HHS R01 GM025508NIGMS NIH HHS R01 GM078666
6 · The paper itself

Abstract

Yeast Mrc1, ortholog of metazoan Claspin, is both a central component of normal DNA replication forks and a mediator of the S phase checkpoint. We report that Mrc1 interacts with Pol2, the catalytic subunit of DNA polymerase epsilon, essential for leading-strand DNA replication and for the checkpoint. In unperturbed cells, Mrc1 interacts independently with both the N-terminal and C-terminal halves of Pol2 (Pol2N and Pol2C). Strikingly, phosphorylation of Mrc1 during the S phase checkpoint abolishes Pol2N binding, but not Pol2C interaction. Mrc1 is required to stabilize Pol2 at replication forks stalled in HU. The bimodal Mrc1/Pol2 interaction may be an additional step in regulating the S phase checkpoint response to DNA damage on the leading strand. We propose that Mrc1, which also interacts with the MCMs, may modulate coupling of polymerization and unwinding at the replication fork.

Indexed as

DNA ReplicationCell Cycle ProteinsChromosomal Proteins, Non-HistoneDNA, FungalDNA HelicasesDNA Polymerase IIFungal ProteinsGenes, FungalModels, MolecularMultiprotein ComplexesMutationPhosphorylationProtein Interaction Domains and MotifsProtein Structure, TertiaryRecombinant ProteinsSaccharomyces cerevisiaeCell Cycle ProteinsChromosomal Proteins, Non-HistoneDNA, FungalDNA HelicasesDNA Polymerase IIFungal ProteinsMCM2 protein, S cerevisiaeMRC1 protein, S cerevisiaeMultiprotein ComplexesRecombinant ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID18851837
PMCPMC2699584
OpenAlexW2123847083

What OpenQuestion holds

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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.