Evidence map›Paper›PMID 28973436›Full record

ArticleNucleic acids research2017

Dual function of Swc5 in SWR remodeling ATPase activation and histone H2A eviction.

Lu Sun, Ed Luk

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

22 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
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  9. Cells · 2023
    Article
  10. Article
  11. Article
  12. Article
  13. Structure and Function of Chromatin Remodelers.Journal of molecular biology · 2021
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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
  19. Article
  20. Article
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

2 authors at 1 institution in 1 country.

Lu SunDepartment of Biochemistry and Cell Biology, Stony Brook University, NY 11794-5215, USA.
Ed LukDepartment of Biochemistry and Cell Biology, Stony Brook University, NY 11794-5215, USA.
Stony Brook University · US

Funding

Mechanisms of chromatin remodeling at yeast promotersR01GM104111 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI LUK, EDWARD E · 2013 to 2022
$2.8M
NIGMS NIH HHS R01 GM104111
6 · The paper itself

Abstract

The chromatin remodeler SWR deposits histone H2A.Z at promoters and other regulatory sites via an ATP-driven histone exchange reaction that replaces nucleosomal H2A with H2A.Z. Simultaneous binding of SWR to both H2A nucleosome and free H2A.Z induces SWR ATPase activity and engages the histone exchange mechanism. Swc5 is a conserved subunit of the 14-polypeptide SWR complex that is required for the histone exchange reaction, but its molecular role is unknown. We found that Swc5, although not required for substrate binding, is required for SWR ATPase stimulation, suggesting that Swc5 is required to couple substrate recognition to ATPase activation. A biochemical complementation assay was developed to show that a unique, conserved domain at the C-terminus of Swc5, called Bucentaur (BCNT), is essential for the histone exchange activity of SWR, whereas an acidic region at the N-terminus is required for optimal SWR function. In vitro studies showed the acidic N-terminus of Swc5 preferentially binds to the H2A-H2B dimer and exhibits histone chaperone activity. We propose that an auxiliary function of Swc5 in SWR is to assist H2A ejection as H2A.Z is inserted into the nucleosome.

Indexed as

Gene Expression Regulation, FungalAdenosine TriphosphatasesChromatin Assembly and DisassemblyGenetic Complementation TestHistone AcetyltransferasesHistonesNucleosomesProtein DomainsProtein IsoformsProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesHistone AcetyltransferasesHistonesNucleosomesProtein IsoformsSaccharomyces cerevisiae Proteins

Identifiers

PMID28973436
PMCPMC5622370
OpenAlexW2735760452

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.