Evidence map›Paper›PMID 26167883›Full record

ArticleNature structural & molecular biology2015

A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks.

Hongda Huang, Caroline B Strømme, Giulia Saredi, Martina Hödl, Anne Strandsby, Cristina González-Aguilera, Shoudeng Chen, Anja Groth, Dinshaw J Patel

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 156 papers.

0numbers the graph read from it
0cells of the map it votes in
156citing papers in PubMed
11.1field-weighted citation impact, top 1% 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

156 citing papers in PubMed, 239 citations in OpenAlex.

  1. Structure and function of the centromere and inner kinetochore.Nature reviews. Molecular cell biology · 2026
    Review
  2. Article
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  5. HAT1 Regulates Intestinal Stem Cell Proliferation and Differentiation.bioRxiv : the preprint server for biology · 2026
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
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  13. Preserving centromere identity: right amounts of CENP-A at the right place and time.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2025
    Review
  14. Review
  15. Article
  16. Review
  17. Review
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  19. Article
  20. Article

96 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 2 institutions in 2 countries.

Hongda HuangStructural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York, USA.
Caroline B StrømmeBiotech Research and Innovation Centre (BRIC) Centre for Epigenetics, University of Copenhagen, Copenhagen, Denmark.
Giulia SarediBiotech Research and Innovation Centre (BRIC) Centre for Epigenetics, University of Copenhagen, Copenhagen, Denmark.
Martina HödlBiotech Research and Innovation Centre (BRIC) Centre for Epigenetics, University of Copenhagen, Copenhagen, Denmark.
Anne StrandsbyBiotech Research and Innovation Centre (BRIC) Centre for Epigenetics, University of Copenhagen, Copenhagen, Denmark.
Cristina González-AguileraBiotech Research and Innovation Centre (BRIC) Centre for Epigenetics, University of Copenhagen, Copenhagen, Denmark.
Shoudeng ChenStructural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York, USA.
Anja GrothBiotech Research and Innovation Centre (BRIC) Centre for Epigenetics, University of Copenhagen, Copenhagen, Denmark.
Dinshaw J PatelStructural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York, USA.
University of Copenhagen · DKMemorial Sloan Kettering Cancer Center · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Nicholas D Socci · 1985 to 2026
$347.4M
NCI NIH HHS P30 CA008748
6 · The paper itself

Abstract

During DNA replication, chromatin is reassembled by recycling of modified old histones and deposition of new ones. How histone dynamics integrates with DNA replication to maintain genome and epigenome information remains unclear. Here, we reveal how human MCM2, part of the replicative helicase, chaperones histones H3-H4. Our first structure shows an H3-H4 tetramer bound by two MCM2 histone-binding domains (HBDs), which hijack interaction sites used by nucleosomal DNA. Our second structure reveals MCM2 and ASF1 cochaperoning an H3-H4 dimer. Mutational analyses show that the MCM2 HBD is required for MCM2-7 histone-chaperone function and normal cell proliferation. Further, we show that MCM2 can chaperone both new and old canonical histones H3-H4 as well as H3.3 and CENPA variants. The unique histone-binding mode of MCM2 thus endows the replicative helicase with ideal properties for recycling histones genome wide during DNA replication.

Indexed as

DNA ReplicationModels, MolecularProtein Structure, TertiaryAmino Acid SequenceBlotting, WesternCell Line, TumorChromatinDNAHeLa CellsHistonesHumansMinichromosome Maintenance Complex Component 2Molecular ChaperonesMolecular Sequence DataMutationNucleic Acid ConformationChromatinDNAHistonesMCM2 protein, humanMinichromosome Maintenance Complex Component 2Molecular Chaperones

Identifiers

PMID26167883
PMCPMC4685956
OpenAlexW2151243552

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.