Evidence map›Paper›PMID 23417676›Full record

ArticleThe Journal of biological chemistry2013

Structure of the Spt16 middle domain reveals functional features of the histone chaperone FACT.

David J Kemble, Frank G Whitby, Howard Robinson, Laura L McCullough, Tim Formosa, Christopher P Hill

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

38 citing papers in PubMed, 59 citations in OpenAlex.

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  18. Structure and function of the histone chaperone FACT - Resolving FACTual issues.Biochimica et biophysica acta. Gene regulatory mechanisms · 2018
    Review
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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 1 country.

David J KembleDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, Utah 84112-5650, USA.
Frank G Whitby
Howard Robinson
Laura L McCullough
Tim Formosa
Christopher P Hill
University of Utah · USBrookhaven National Laboratory · US

Funding

Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
Biochemical, Genetic, and Genomic Analysis of Nucleosome Reorganization by FACTR01GM064649 · NIGMS · UNIVERSITY OF UTAH · PI FORMOSA, TIMOTHY G · 2002 to 2022
$6.4M
Structures of Proteasome ActivatorsR01GM059135 · NIGMS · UNIVERSITY OF UTAH · PI HILL, CHRISTOPHER P. · 1999 to 2012
$3.4M
NIBIB NIH HHS P30 EB009998NIGMS NIH HHS GM064649NIGMS NIH HHS R01 GM059135NIGMS NIH HHS R01 GM064649NIGMS NIH HHS R01 GM59135
6 · The paper itself

Abstract

The histone chaperone FACT is an essential and abundant heterodimer found in all eukaryotes. Here we report a crystal structure of the middle domain of the large subunit of FACT (Spt16-M) to reveal a double pleckstrin homology architecture. This structure was found previously in the Pob3-M domain of the small subunit of FACT and in the related histone chaperone Rtt106, although Spt16-M is distinguished from these structures by the presence of an extended α-helix and a C-terminal addition. Consistent with our finding that the double pleckstrin homology structure is common to these three histone chaperones and reports that Pob3 and Rtt106 double pleckstrin homology domains bind histones H3-H4, we also find that Spt16-M binds H3-H4 with low micromolar affinity. Our structure provides a framework for interpreting a large body of genetic data regarding the physiological functions of FACT, including the identification of potential interaction surfaces for binding histones or other proteins.

Indexed as

AnimalsCrystallography, X-RayDNA-Binding ProteinsHigh Mobility Group ProteinsHumansMolecular ChaperonesProtein Structure, SecondaryProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStructural Homology, ProteinStructure-Activity RelationshipTranscriptional Elongation FactorsTranscription FactorsDNA-Binding ProteinsFACT protein, S cerevisiaeHigh Mobility Group ProteinsMolecular ChaperonesPOB3 protein, S cerevisiaeRtt106 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSPT16 protein, S cerevisiaeTranscriptional Elongation FactorsTranscription Factors

Identifiers

PMID23417676
PMCPMC3624403
OpenAlexW2008326196

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.