Evidence map›Paper›PMID 16260604›Full record

ArticleMolecular and cellular biology2005

The histone fold subunits of Drosophila CHRAC facilitate nucleosome sliding through dynamic DNA interactions.

Klaus F Hartlepp, Carlos Fernández-Tornero, Anton Eberharter, Tim Grüne, Christoph W Müller, Peter B Becker

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

35 citing papers in PubMed, 75 citations in OpenAlex.

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  11. TheFrontiers in plant science · 2016
    Review
  12. The architecture of a eukaryotic replisome.Nature structural & molecular biology · 2015
    Article
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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 2 institutions in 2 countries.

Klaus F HartleppEuropean Molecular Biology Laboratory, Grenoble Outstation, France.
Carlos Fernández-Tornero
Anton Eberharter
Tim Grüne
Christoph W Müller
Peter B Becker
European Molecular Biology Laboratory · FRLudwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The chromatin accessibility complex (CHRAC) is an abundant, evolutionarily conserved nucleosome remodeling machinery able to catalyze histone octamer sliding on DNA. CHRAC differs from the related ACF complex by the presence of two subunits with molecular masses of 14 and 16 kDa, whose structure and function were not known. We determined the structure of Drosophila melanogaster CHRAC14-CHRAC16 by X-ray crystallography at 2.4-angstroms resolution and found that they dimerize via a variant histone fold in a typical handshake structure. In further analogy to histones, CHRAC14-16 contain unstructured N- and C-terminal tail domains that protrude from the handshake structure. A dimer of CHRAC14-16 can associate with the N terminus of ACF1, thereby completing CHRAC. Low-affinity interactions of CHRAC14-16 with DNA significantly improve the efficiency of nucleosome mobilization by limiting amounts of ACF. Deletion of the negatively charged C terminus of CHRAC16 enhances DNA binding 25-fold but leads to inhibition of nucleosome sliding, in striking analogy to the effect of the DNA chaperone HMGB1 on nucleosome sliding. The presence of a surface compatible with DNA interaction and the geometry of an H2A-H2B heterodimer may provide a transient acceptor site for DNA dislocated from the histone surface and therefore facilitate the nucleosome remodeling process.

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceAnimalsCatalysisCloning, MolecularCrystallography, X-RayDimerizationDNADrosophila ProteinsEscherichia coliGene DeletionGlutathione TransferaseHistonesHumansModels, MolecularMolecular Sequence DataAcf protein, DrosophilaAdenosine TriphosphatasesCHRAC-14 protein, DrosophilaCHRAC-16 protein, DrosophilaDNADrosophila ProteinsGlutathione TransferaseHistonesNucleoproteinsNucleosomesTranscription Factors

Identifiers

PMID16260604
PMCPMC1280263
OpenAlexW2116990889

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.