Evidence map›Paper›PMID 19822659›Full record

ArticleMolecular and cellular biology2009

Two fundamentally distinct PCNA interaction peptides contribute to chromatin assembly factor 1 function.

Tom Rolef Ben-Shahar, Araceli G Castillo, Michael J Osborne, Katherine L B Borden, Jack Kornblatt, Alain Verreault

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

58 citing papers in PubMed, 87 citations in OpenAlex.

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  8. Acute multi-level response to defectivebioRxiv : the preprint server for biology · 2024
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  17. Unorthodox PCNA Binding by Chromatin Assembly Factor 1.International journal of molecular sciences · 2022
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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

6 authors at 5 institutions in 3 countries.

Tom Rolef Ben-ShaharCancer Research UK, London Research Institute, London WC2A 3PX, United Kingdom.
Araceli G Castillo
Michael J Osborne
Katherine L B Borden
Jack Kornblatt
Alain Verreault
Université de Montréal · CACancer Research UK · GBConcordia University · CAInstitute for Research in Immunology and Cancer · CAUniversidad de Málaga · ES

Funding

Canadian Institutes of Health Research FRN 89928Cancer Research UK
6 · The paper itself

Abstract

Chromatin assembly factor 1 (CAF-1) deposits histones H3 and H4 rapidly behind replication forks through an interaction with the proliferating cell nuclear antigen (PCNA), a DNA polymerase processivity factor that also binds to a number of replication enzymes and other proteins that act on nascent DNA. The mechanisms that enable CAF-1 and other PCNA-binding proteins to function harmoniously at the replication fork are poorly understood. Here we report that the large subunit of human CAF-1 (p150) contains two distinct PCNA interaction peptides (PIPs). The N-terminal PIP binds strongly to PCNA in vitro but, surprisingly, is dispensable for nucleosome assembly and only makes a modest contribution to targeting p150 to DNA replication foci in vivo. In contrast, the internal PIP (PIP2) lacks one of the highly conserved residues of canonical PIPs and binds weakly to PCNA. Surprisingly, PIP2 is essential for nucleosome assembly during DNA replication in vitro and plays a major role in targeting p150 to sites of DNA replication. Unlike canonical PIPs, such as that of p21, the two p150 PIPs are capable of preferentially inhibiting nucleosome assembly, rather than DNA synthesis, suggesting that intrinsic features of these peptides are part of the mechanism that enables CAF-1 to function behind replication forks without interfering with other PCNA-mediated processes.

Indexed as

DNA ReplicationAmino Acid SequenceAnimalsCell LineChromatin Assembly Factor-1HeterochromatinHumansMiceModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedNucleosomesPeptidesProliferating Cell Nuclear AntigenProtein Structure, TertiaryProtein SubunitsChromatin Assembly Factor-1CNOT8 protein, humanHeterochromatinNucleosomesPeptidesProliferating Cell Nuclear AntigenProtein SubunitsTranscription Factors

Identifiers

PMID19822659
PMCPMC2786881
OpenAlexW2156875872

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.