Evidence map›Paper›PMID 19223330›Full record

ArticleNucleic acids research2009

Solution structure of a novel zinc finger motif in the SAP30 polypeptide of the Sin3 corepressor complex and its potential role in nucleic acid recognition.

Yuan He, Rebecca Imhoff, Anirban Sahu, Ishwar Radhakrishnan

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

12 citing papers in PubMed, 20 citations in OpenAlex.

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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

4 authors at 1 institution in 1 country.

Yuan HeDepartment of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, IL 60208-3500, USA.
Rebecca Imhoff
Anirban Sahu
Ishwar Radhakrishnan
Northwestern University · US

Funding

Structural Biology of the Sin3 Corepressor ComplexR01GM064715 · NIGMS · NORTHWESTERN UNIVERSITY · PI RADHAKRISHNAN, ISHWAR · 2002 to 2011
$2.4M
STRUCTURAL BIOL RES: LUNG SURFACTANT PROTEINS, DISTRESSS10RR019071 · NCRR · NORTHWESTERN UNIVERSITY · PI RADHAKRISHNAN, ISHWAR · 2005 to 2005
$272k
NCRR NIH HHS S10 RR019071NIGMS NIH HHS GM64715NIGMS NIH HHS R01 GM064715
6 · The paper itself

Abstract

Giant chromatin-modifying complexes regulate gene transcription in eukaryotes by acting on chromatin substrates and 'setting' the histone code. The histone deacetylase (HDAC)-associated mammalian Sin3 corepressor complex regulates a wide variety of genes involved in all aspects of cellular physiology. The recruitment of the corepressor complex by transcription factors to specific regions of the genome is mediated by Sin3 as well as 10 distinct polypeptides that comprise the corepressor complex. Here we report the solution structure of a novel CCCH zinc finger (ZnF) motif in the SAP30 polypeptide, a key component of the corepressor complex. The structure represents a novel fold comprising two beta-strands and two alpha-helices with the zinc organizing center showing remote resemblance to the treble clef motif. In silico analysis of the structure revealed a highly conserved surface that is dominated by basic residues. NMR-based analysis of potential ligands for the SAP30 ZnF motif indicated a strong preference for nucleic acid substrates. We propose that the SAP30 ZnF functions as a double-stranded DNA-binding motif, thereby expanding the known functions of both SAP30 and the mammalian Sin3 corepressor complex. Our results also call into question the common assumption about the exclusion of DNA-binding core subunits within chromatin-modifying/remodeling complexes.

Indexed as

Zinc FingersAmino Acid SequenceDNADNA-Binding ProteinsHistone DeacetylasesModels, MolecularMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularNuclear ProteinsProtein BindingProtein FoldingRepressor ProteinsSin3 Histone Deacetylase and Corepressor ComplexStructure-Activity RelationshipTranscription FactorsDNADNA-Binding ProteinsHistone DeacetylasesNuclear ProteinsRepressor ProteinsSAP30BP protein, humanSin3 Histone Deacetylase and Corepressor ComplexTranscription Factors

Identifiers

PMID19223330
PMCPMC2673417
OpenAlexW2061536768

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.