Evidence map›Paper›PMID 30970243›Full record

ArticleCell reports2019

Transient Kinetic Analysis of SWR1C-Catalyzed H2A.Z Deposition Unravels the Impact of Nucleosome Dynamics and the Asymmetry of Histone Exchange.

Raushan K Singh, Jiayl Fan, Nathan Gioacchini, Shinya Watanabe, Osman Bilsel, Craig L Peterson

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

23 citing papers in PubMed, 37 citations in OpenAlex.

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  16. Structure and Function of Chromatin Remodelers.Journal of molecular biology · 2021
    Review
  17. Review
  18. Review
  19. Role of a DEF/Y motif in histone H2A-H2B recognition and nucleosome editing.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  20. H2A Variants inPlant communications · 2020
    Review
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 1 institution in 1 country.

Raushan K SinghProgram in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Jiayl FanProgram in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Nathan GioacchiniProgram in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Shinya WatanabeProgram in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Osman BilselDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01655, USA.
Craig L PetersonProgram in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA. Electronic address: craig.peterson@umassmed.edu.
University of Massachusetts Chan Medical School · US

Funding

Regulation of chromatin dynamicsR35GM122519 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI Craig L Peterson · 2017 to 2026
$9.2M
Analysis of the yeast SWI1, SWI2, and SWI3 proteinsR37GM049650 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI PETERSON, CRAIG L · 2006 to 2015
$4.9M
YEAST SWI1, SWI2, AND SWI3 PROTEINSR01GM049650 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI PETERSON, CRAIG L · 1993 to 2016
$2.6M
NIGMS NIH HHS R01 GM049650NIGMS NIH HHS R35 GM122519NIGMS NIH HHS R37 GM049650
6 · The paper itself

Abstract

The SWR1C chromatin remodeling enzyme catalyzes ATP-dependent replacement of nucleosomal H2A with the H2A.Z variant, regulating key DNA-mediated processes such as transcription and DNA repair. Here, we investigate the transient kinetic mechanism of the histone exchange reaction, employing ensemble FRET, fluorescence correlation spectroscopy (FCS), and the steady-state kinetics of ATP hydrolysis. Our studies indicate that SWR1C modulates nucleosome dynamics on both the millisecond and microsecond timescales, poising the nucleosome for the dimer exchange reaction. The transient kinetic analysis of the remodeling reaction performed under single turnover conditions unraveled a striking asymmetry in the ATP-dependent replacement of nucleosomal dimers, promoted by localized DNA unwrapping. Taken together, our transient kinetic studies identify intermediates and provide crucial insights into the SWR1C-catalyzed dimer exchange reaction and shed light on how the mechanics of H2A.Z deposition might contribute to transcriptional regulation in vivo.

Indexed as

Chromatin Assembly and DisassemblyAnimalsCatalysisHistonesHumansNucleosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsXenopus laevisHistonesNucleosomesSaccharomyces cerevisiae ProteinschromatinFCSFRETH2A.ZnucleosomeSWR1Ctranscription

Identifiers

PMID30970243
PMCPMC6545893
OpenAlexW2949546450

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.