Evidence map›Paper›PMID 11003645›Full record

ArticleMolecular and cellular biology2000

SAF-Box, a conserved protein domain that specifically recognizes scaffold attachment region DNA.

M Kipp, F Göhring, T Ostendorp, C M van Drunen, R van Driel, M Przybylski, F O Fackelmayer

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
5.5field-weighted citation impact, top 3% 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

84 citing papers in PubMed, 194 citations in OpenAlex.

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  9. Nuclear architecture and the structural basis of mitotic memory.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2023
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  14. MRTF: Basic Biology and Role in Kidney Disease.International journal of molecular sciences · 2021
    Review
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  20. Review

24 more citing papers are in PubMed but not listed here.

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

7 authors at 4 institutions in 3 countries.

M KippDepartment of Biology, University of Konstanz, 78434 Konstanz, Germany.
F Göhring
T Ostendorp
C M van Drunen
R van Driel
M Przybylski
F O Fackelmayer
GATC Biotech (Germany) · DEUniversity of Amsterdam · NLUniversity of Birmingham · GBUniversity of Konstanz · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SARs (scaffold attachment regions) are candidate DNA elements for partitioning eukaryotic genomes into independent chromatin loops by attaching DNA to proteins of a nuclear scaffold or matrix. The interaction of SARs with the nuclear scaffold is evolutionarily conserved and appears to be due to specific DNA binding proteins that recognize SARs by a mechanism not yet understood. We describe a novel, evolutionarily conserved protein domain that specifically binds to SARs but is not related to SAR binding motifs of other proteins. This domain was first identified in human scaffold attachment factor A (SAF-A) and was thus designated SAF-Box. The SAF-Box is present in many different proteins ranging from yeast to human in origin and appears to be structurally related to a homeodomain. We show here that SAF-Boxes from four different origins, as well as a synthetic SAF-Box peptide, bind to natural and artificial SARs with high specificity. Specific SAR binding of the novel domain is achieved by an unusual mass binding mode, is sensitive to distamycin but not to chromomycin, and displays a clear preference for long DNA fragments. This is the first characterization of a specific SAR binding domain that is conserved throughout evolution and has DNA binding properties that closely resemble that of the unfractionated nuclear scaffold.

Indexed as

Conserved SequenceAmino Acid MotifsAmino Acid SequenceAnimalsBinding SitesCell LineChromatinChromomycinsCloning, MolecularDistamycinsDNADNA-Binding ProteinsHumansMolecular Sequence DataMutationNuclear ProteinsChromatinChromomycinsDistamycinsDNADNA-Binding ProteinsNuclear ProteinsOligodeoxyribonucleotidesPeptide FragmentsRecombinant Proteinsstallimycin

Identifiers

PMID11003645
PMCPMC86301
OpenAlexW2170517581

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.