Evidence map›Paper›PMID 20853842›Full record

ArticleBiochemistry2010

The ATP-dependent remodeler RSC transfers histone dimers and octamers through the rapid formation of an unstable encounter intermediate.

Claire E Rowe, Geeta J Narlikar

Abstract read
In one paragraph

Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.3field-weighted citation impact, top 41% 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

18 citing papers in PubMed, 27 citations in OpenAlex.

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  15. Preparation and analysis of positioned mononucleosomes.Methods in molecular biology (Clifton, N.J.) · 2015
    Article
  16. Article
  17. Article
  18. Swi2/Snf2 remodelers: hybrid views on hybrid molecular machines.Current opinion in structural biology · 2012
    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

2 authors at 1 institution in 1 country.

Claire E RoweDepartment of Biochemistry and Biophysics, University of California, San Francisco, California 94158, USA.
Geeta J Narlikar
University of California, San Francisco · US

Funding

Mechanistic Analysis of Chromatin RemodelingR01GM073767 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI NARLIKAR, GEETA J · 2005 to 2018
$4.7M
NIGMS NIH HHS R01 GM073767
6 · The paper itself

Abstract

RSC, an essential chromatin remodeling complex in budding yeast, is involved in a variety of biological processes including transcription, recombination, repair, and replication. How RSC participates in such diverse processes is not fully understood. In vitro, RSC uses ATP to carry out several seemingly distinct reactions: it repositions nucleosomes, transfers H2A/H2B dimers between nucleosomes, and transfers histone octamers between pieces of DNA. This raises the intriguing mechanistic question of how this molecular machine can use a single ATPase subunit to create these varied products. Here, we use a FRET-based approach to kinetically order the products of the RSC reaction. Surprisingly, transfer of H2A/H2B dimers and histone octamers is initiated on a time scale of seconds when assayed by FRET, but formation of stable nucleosomal products occurs on a time scale of minutes when assayed by native gel. These results suggest a model in which RSC action rapidly generates an unstable encounter intermediate that contains the two exchange substrates in close proximity. This intermediate then collapses more slowly to form the stable transfer products seen on native gels. The rapid, biologically relevant time scale on which the transfer products are generated implies that such products can play key roles in vivo.

Indexed as

Adenosine TriphosphateAnimalsChromatinDimerizationDNA-Binding ProteinsDNA RepairDNA ReplicationFluorescence Resonance Energy TransferHistonesKineticsNuclear ProteinsNucleosomesRecombinant ProteinsRecombination, GeneticSaccharomyces cerevisiae ProteinsTranscription FactorsAdenosine TriphosphateChromatinDNA-Binding ProteinsHistonesNuclear ProteinsNucleosomesRecombinant ProteinsRSC complex, S cerevisiaeSaccharomyces cerevisiae ProteinsTranscription Factors

Identifiers

PMID20853842
PMCPMC2976819
OpenAlexW2028483312

What OpenQuestion holds

Textmetadata
LicenceTDM
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.