Evidence map›Paper›PMID 19273607›Full record

ArticleMolecular and cellular biology2009

Nucleosome remodeling and transcriptional repression are distinct functions of Isw1 in Saccharomyces cerevisiae.

Marina Pinskaya, Anitha Nair, David Clynes, Antonin Morillon, Jane Mellor

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed, 34 citations in OpenAlex.

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  8. Nucleosome sliding mechanisms: new twists in a looped history.Nature structural & molecular biology · 2013
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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

5 authors at 3 institutions in 2 countries.

Marina PinskayaDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, United Kingdom.
Anitha Nair
David Clynes
Antonin Morillon
Jane Mellor
University of Oxford · GBCentre de Génétique Moléculaire · FRCentre National de la Recherche Scientifique · FR

Funding

Wellcome Trust
6 · The paper itself

Abstract

The SANT domain is a nucleosome recognition module found in transcriptional regulatory proteins, including chromatin-modifying enzymes. It shows high functional degeneracy between species, varying in sequence and copy number. Here, we investigate functions in vivo associated with two SANT motifs, SANT and SLIDE, in the Saccharomyces cerevisiae Isw1 chromatin-remodeling ATPase. We show that differences in the primary structures of the SANT and SLIDE domains in yeast and Drosophila melanogaster reflect their different functions. In yeast, the SLIDE domain is required for histone interactions, while this is a function of the SANT domain in flies. In yeast, both motifs are required for optimal association with chromatin and for formation of the Isw1b complex (Isw1, Ioc2, and Ioc4). Moreover, nucleosome remodeling at the MET16 locus is defective in strains lacking the SANT or SLIDE domain. In contrast, the SANT domain is dispensable for the interaction between Isw1 and Ioc3 in the Isw1a complex. We show that, although defective in nucleosome remodeling, Isw1 lacking the SANT domain is able to repress transcription initiation at the MET16 promoter. Thus, chromatin remodeling and transcriptional repression are distinct activities of Isw1.

Indexed as

Chromatin Assembly and DisassemblyGene Expression Regulation, FungalSaccharomyces cerevisiaeAdenosine TriphosphatasesAmino Acid SequenceAnimalsDNA-Binding ProteinsDrosophila melanogasterDrosophila ProteinsHistonesModels, MolecularMolecular Sequence DataNucleosomesOxidoreductasesProtein Structure, TertiarySaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesDNA-Binding ProteinsDrosophila ProteinsHistonesIOC2 protein, S cerevisiaeIOC4 protein, S cerevisiaeISW1 protein, S cerevisiaeMET16 protein, S cerevisiaeNucleosomesOxidoreductasesSaccharomyces cerevisiae Proteins

Identifiers

PMID19273607
PMCPMC2668368
OpenAlexW2140428119

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.