Evidence map›Paper›PMID 26109053›Full record

ArticleGenes & development2015

Structure-function studies of histone H3/H4 tetramer maintenance during transcription by chaperone Spt2.

Shoudeng Chen, Anne Rufiange, Hongda Huang, Kanagalaghatta R Rajashankar, Amine Nourani, Dinshaw J Patel

Abstract read
In one paragraph

Article in Genes & development, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
–field-weighted citation impact
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

27 citing papers in PubMed.

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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.

Shoudeng ChenStructural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10065, USA;
Anne RufiangeGroupe St-Patrick de Recherche en Oncologie Fondamentale, L'Hôtel-Dieu de Québec (Université Laval), Québec G1R 2J6, Canada;
Hongda HuangStructural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10065, USA;
Kanagalaghatta R RajashankarNortheastern Collaborative Access Team (NE-CAT), Advanced Photon Source, Argonne National Laboratory, Chicago, Illinois 60439, USA; Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, USA.
Amine NouraniGroupe St-Patrick de Recherche en Oncologie Fondamentale, L'Hôtel-Dieu de Québec (Université Laval), Québec G1R 2J6, Canada;
Dinshaw J PatelStructural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10065, USA;

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Nicholas D Socci · 1985 to 2026
$347.4M
Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
Canadian Institutes of Health Research MOP81245NCI NIH HHS P30 CA008748NCRR NIH HHS S10 RR029205NIGMS NIH HHS P41 GM103403
6 · The paper itself

Abstract

Cells use specific mechanisms such as histone chaperones to abrogate the inherent barrier that the nucleosome poses to transcribing polymerases. The current model postulates that nucleosomes can be transiently disrupted to accommodate passage of RNA polymerases and that histones H3 and H4 possess their own chaperones dedicated to the recovery of nucleosomes. Here, we determined the crystal structure of the conserved C terminus of human Suppressors of Ty insertions 2 (hSpt2C) chaperone bound to an H3/H4 tetramer. The structural studies demonstrate that hSpt2C is bound to the periphery of the H3/H4 tetramer, mimicking the trajectory of nucleosomal-bound DNA. These structural studies have been complemented with in vitro binding and in vivo functional studies on mutants that disrupt key intermolecular contacts involving two acidic patches and hydrophobic residues on Spt2C. We show that contacts between both human and yeast Spt2C with the H3/H4 tetramer are required for the suppression of H3/H4 exchange as measured by H3K56ac and new H3 deposition. These interactions are also crucial for the inhibition of spurious transcription from within coding regions. Together, our data indicate that Spt2 interacts with the periphery of the H3/H4 tetramer and promotes its recycling in the wake of RNA polymerase.

Indexed as

Models, MolecularChromosomal Proteins, Non-HistoneDNA-Binding ProteinsGene Expression RegulationHistone ChaperonesHistonesMultiprotein ComplexesNucleosomesProtein BindingProtein StabilityProtein Structure, QuaternarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSaltsStructure-Activity RelationshipTranscription, GeneticChromosomal Proteins, Non-HistoneDNA-Binding ProteinsHistone ChaperonesHistonesMultiprotein ComplexesNucleosomesSaccharomyces cerevisiae ProteinsSaltsSPT2 protein, S cerevisiaeSPTY2D1 protein, humanepigeneticsH3/H4 tetramerhistone chaperonehistone maintenanceSpt2spurious transcriptiontranscription elongation

Identifiers

PMID26109053
PMCPMC4495402

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Registered trials

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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.