Evidence map›Paper›PMID 9001253›Full record

ArticleMolecular and cellular biology1997

The scs' boundary element: characterization of boundary element-associated factors.

C M Hart, K Zhao, U K Laemmli

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In one paragraph

Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

56 citing papers in PubMed.

  1. TheGenes · 2026
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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

3 authors.

C M HartDepartment of Biochemistry, University of Geneva, Switzerland.
K Zhao
U K Laemmli

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Boundary elements are thought to define the peripheries of chromatin domains and to restrict enhancer-promoter interactions to their target genes within their domains. We previously characterized a cDNA encoding the BEAF-32A protein (32A), which binds with high affinity to the scs' boundary element from the Drosophila melanogaster 87A7 hsp70 locus. Here, we report a second protein, BEAF-32B, that differs from 32A only in its amino terminus. Unlike 32A, it has the same DNA binding specificity as the complete BEAF activity affinity purified from Drosophila. We characterize three domains in these proteins. Heterocomplex formation is mediated by their identical carboxy-terminal domains, and DNA binding is mediated by their unique amino-terminal domains. The identical middle domains of 32A and 32B are dispensable for the functions described here, although they may be important for boundary element function. 32A and 32B apparently form trimers, and the ratio of 32A to 32B varies at different loci on polytene chromosomes as judged by immunofluorescence. The scs' element contains a high- and low-affinity binding site for BEAF. We observed that interaction with the low-affinity site is facilitated by binding to the high-affinity site some 200 bp distant.

Indexed as

Drosophila ProteinsEye ProteinsAmino Acid SequenceAnimalsChromatinChromosomesCloning, MolecularDimerizationDNADNA-Binding ProteinsDNA, ComplementaryDrosophila melanogasterMolecular Sequence DataMolecular WeightProtein BindingRecombinant Fusion ProteinsBEAF-32 protein, DrosophilaChromatinDNADNA-Binding ProteinsDNA, ComplementaryDrosophila ProteinsEye ProteinsRecombinant Fusion Proteins

Identifiers

PMID9001253
PMCPMC231825

What OpenQuestion holds

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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.