Evidence map›Paper›PMID 27397685›Full record

ArticleMolecular cell2016

Ctf4 Is a Hub in the Eukaryotic Replisome that Links Multiple CIP-Box Proteins to the CMG Helicase.

Fabrizio Villa, Aline C Simon, Maria Angeles Ortiz Bazan, Mairi L Kilkenny, David Wirthensohn, Mel Wightman, Dijana Matak-Vinkovíc, Luca Pellegrini, Karim Labib

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
9.2field-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

79 citing papers in PubMed, 127 citations in OpenAlex.

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  12. Specialized replication of heterochromatin domains ensures self-templated chromatin assembly and epigenetic inheritance.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  20. The TIMELESS effort for timely DNA replication and protection.Cellular and molecular life sciences : CMLS · 2023
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19 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 1 country.

Fabrizio VillaMRC Protein Phosphorylation and Ubiquitylation Unit, Sir James Black Centre, School of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, UK.
Aline C SimonDepartment of Biochemistry, University of Cambridge, 80, Tennis Court Road, Cambridge CB2 1GA, UK.
Maria Angeles Ortiz BazanMRC Protein Phosphorylation and Ubiquitylation Unit, Sir James Black Centre, School of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, UK.
Mairi L KilkennyDepartment of Biochemistry, University of Cambridge, 80, Tennis Court Road, Cambridge CB2 1GA, UK.
David WirthensohnDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Mel WightmanMRC Protein Phosphorylation and Ubiquitylation Unit, Sir James Black Centre, School of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, UK.
Dijana Matak-VinkovícDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Luca PellegriniDepartment of Biochemistry, University of Cambridge, 80, Tennis Court Road, Cambridge CB2 1GA, UK. Electronic address: lp212@cam.ac.uk.
Karim LabibMRC Protein Phosphorylation and Ubiquitylation Unit, Sir James Black Centre, School of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, UK. Electronic address: kpmlabib@dundee.ac.uk.
University of Cambridge · GBMRC Protein Phosphorylation and Ubiquitylation Unit · GBUniversity of Dundee · GB

Funding

Medical Research Council MC_UU_12016/13Wellcome Trust 097945/B/11/ZWellcome Trust 102943Wellcome Trust 102943/Z/13/ZWellcome Trust 104641/Z/14/Z
6 · The paper itself

Abstract

Replisome assembly at eukaryotic replication forks connects the DNA helicase to DNA polymerases and many other factors. The helicase binds the leading-strand polymerase directly, but is connected to the Pol α lagging-strand polymerase by the trimeric adaptor Ctf4. Here, we identify new Ctf4 partners in addition to Pol α and helicase, all of which contain a "Ctf4-interacting-peptide" or CIP-box. Crystallographic analysis classifies CIP-boxes into two related groups that target different sites on Ctf4. Mutations in the CIP-box motifs of the Dna2 nuclease or the rDNA-associated protein Tof2 do not perturb DNA synthesis genome-wide, but instead lead to a dramatic shortening of chromosome 12 that contains the large array of rDNA repeats. Our data reveal unexpected complexity of Ctf4 function, as a hub that connects multiple accessory factors to the replisome. Most strikingly, Ctf4-dependent recruitment of CIP-box proteins couples other processes to DNA synthesis, including rDNA copy-number regulation.

Indexed as

S PhaseBinding SitesChromosomes, FungalDNA-Binding ProteinsDNA, FungalDNA HelicasesDNA Polymerase IDNA, RibosomalGene DosageIntracellular Signaling Peptides and ProteinsModels, MolecularMultiprotein ComplexesMutationProtein BindingProtein Interaction Domains and MotifsSaccharomyces cerevisiaeCTF4 protein, S cerevisiaeDNA2 protein, S cerevisiaeDNA-Binding ProteinsDNA, FungalDNA HelicasesDNA Polymerase IDNA, RibosomalIntracellular Signaling Peptides and ProteinsMultiprotein ComplexesSaccharomyces cerevisiae ProteinsTOF2 protein, S cerevisiae

Identifiers

PMID27397685
PMCPMC4980431
OpenAlexW2472184758

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.