Linked Life Data

8444154

Source:http://linkedlifedata.com/resource/pubmed/id/8444154

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1993-4-2
pubmed:databankReference
pubmed:abstractText
Heme oxygenase is an essential enzyme in heme catabolism, and also known as a 32-kDa heat-shock protein in rat. The rat heme-oxygenase gene promoter contains a functional heat-shock element (HSE) designated as HSE1 (-290 to -276 from the transcriptional initiation site), which consists of three copies of a 5-bp unit (5'-NGAAN-3';-->) in alternating orientation. Here we identified a putative HSE (-221 to -212), designated as HSE2, consisting of an inverted repeat of this 5-bp unit (<==>). Using transient expression assays, we show that HSE1 is sufficient to confer the heat-inducibility (a three fold to fourfold increase) on the reporter gene located downstream from the rat heme-oxygenase gene promoter, but HSE2 alone is not, suggesting that HSE2, a HSE of a tail-to-tail configuration, is not functional in vivo. However, the presence of both HSE1 and HSE2 in the promoter region increased the heat-mediated induction of the reporter-gene expression by more than 15-fold. Gel mobility-shift assays indicate that both HSE1 and HSE2 are recognized by activated heat-shock factor present only in heat-shocked rat glioma cells. Interestingly, the sequence containing HSE2 is also bound by a protein that is present in nuclear extracts prepared from either heat-shocked or non-shocked glioma cells, but this nuclear protein is unable to bind to HSE1. We suggest that a protein binding to the sequence containing HSE2 may be involved in transcriptional regulation of the rat heme oxygenase gene under thermal stress.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
212
pubmed:geneSymbol
HSE1, HSE2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
167-75
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:8444154-Animals, pubmed-meshheading:8444154-Base Sequence, pubmed-meshheading:8444154-Binding Sites, pubmed-meshheading:8444154-DNA Probes, pubmed-meshheading:8444154-DNA-Binding Proteins, pubmed-meshheading:8444154-Gene Expression Regulation, Enzymologic, pubmed-meshheading:8444154-HeLa Cells, pubmed-meshheading:8444154-Heat-Shock Proteins, pubmed-meshheading:8444154-Heme Oxygenase (Decyclizing), pubmed-meshheading:8444154-Hot Temperature, pubmed-meshheading:8444154-Humans, pubmed-meshheading:8444154-Mice, pubmed-meshheading:8444154-Molecular Sequence Data, pubmed-meshheading:8444154-Nuclear Proteins, pubmed-meshheading:8444154-Promoter Regions, Genetic, pubmed-meshheading:8444154-Rats, pubmed-meshheading:8444154-Regulatory Sequences, Nucleic Acid, pubmed-meshheading:8444154-Transcription, Genetic
pubmed:year
1993
pubmed:articleTitle
Identification of a nuclear protein that constitutively recognizes the sequence containing a heat-shock element. Its binding properties and possible function modulating heat-shock induction of the rat heme oxygenase gene.
pubmed:affiliation
Department of Applied Physiology and Molecular Biology, Tohoku University School of Medicine, Sendai, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't