Evidence map›Paper›PMID 8497256›Full record

ArticleMolecular and cellular biology1993

Mouse heat shock transcription factors 1 and 2 prefer a trimeric binding site but interact differently with the HSP70 heat shock element.

P E Kroeger, K D Sarge, R I Morimoto

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

39 citing papers in PubMed, 107 citations in OpenAlex.

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  8. Transcriptional response to stress in the dynamic chromatin environment of cycling and mitotic cells.Proceedings of the National Academy of Sciences of the United States of America · 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

3 authors at 1 institution in 1 country.

P E KroegerDepartment of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208-3500.
K D Sarge
R I Morimoto
Northwestern University · US

Funding

REGULATION AND EXPRESSION OF THE HSP70 GENE FAMILYR37GM038109 · NIGMS · NORTHWESTERN UNIVERSITY · PI MORIMOTO, RICHARD I · 2000 to 2009
$5.6M
REGULATION AND EXPRESSION OF THE HUMAN HSP70 GENE FAMILYR01GM038109 · NIGMS · NORTHWESTERN UNIVERSITY · PI MORIMOTO, RICHARD I · 1987 to 2013
$2.2M
NIGMS NIH HHS GM38109
6 · The paper itself

Abstract

To understand the function of multiple heat shock transcription factors in higher eukaryotes, we have characterized the interaction of recombinant mouse heat shock transcription factors 1 and 2 (mHSF1 and mHSF2) with their binding site, the heat shock element (HSE). For our analysis, we utilized the human HSP70 HSE, which consists of three perfect 5'-nGAAn-3' sites (1, 3, and 4) and two imperfect sites (2 and 5) arranged as tandem inverted repeats. Recombinant mHSF1 and mHSF2, which exist as trimers in solution, both bound specifically to this HSE and stimulated transcription of a human HSP70-CAT construct in vitro. Footprinting analyses revealed differential binding of mHSF1 and mHSF2 to the HSP70 HSE. Specifically, mHSF1 bound all five pentameric sites, whereas mHSF2 failed to interact with the first site of the HSE but bound to sites 2 to 5. Missing-nucleoside analysis demonstrated that the third and fourth nGAAn sites were essential for mHSF1 and mHSF2 binding. The binding of the initial mHSF1 trimer to the HSE exhibited preference for sites 3, 4, and 5, and then binding of a second trimer occurred at sites 1 and 2. These results suggest that HSF may recognize its binding site through the dyad symmetry of sites 3 and 4 but requires an adjacent site for stable interaction. Our data demonstrate that mHSF1 and mHSF2 bind specifically to the HSE through major groove interactions. Methidiumpropyl-EDTA footprinting revealed structural differences in the first and third repeats of the HSE, suggesting that the DNA is distorted in this region. The possibility that the HSE region is naturally distorted may assist in understanding how a trimer of HSF can bind to what is essentially an inverted repeat binding site.

Indexed as

Promoter Regions, GeneticAnimalsBase SequenceBinding SitesChloramphenicol O-AcetyltransferaseDeoxyribonuclease IDNADNA-Binding ProteinsHeat-Shock ProteinsHeat Shock Transcription FactorsHumansKineticsMacromolecular SubstancesMiceMolecular Sequence DataNucleic Acid ConformationChloramphenicol O-AcetyltransferaseDeoxyribonuclease IDNADNA-Binding ProteinsHeat-Shock ProteinsHeat Shock Transcription FactorsHSF2 protein, humanMacromolecular SubstancesOligodeoxyribonucleotidesRecombinant ProteinsTranscription Factors

Identifiers

PMID8497256
PMCPMC359798
OpenAlexW1747840667

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.