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Proc Natl Acad Sci U S A
1985 Aug 01;8215:4949-53.
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Isolation and functional analysis of a human 70,000-dalton heat shock protein gene segment.
Voellmy R, Ahmed A, Schiller P, Bromley P, Rungger D.
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A human 70-kDa heat shock protein (hsp70) gene segment has been isolated. The segment contains 3.15 kilobase pairs (kbp) of 5' nontranscribed sequence, an RNA leader of 119 bp, and a protein-coding region of 741 bp. The human protein sequence shows a high degree of homology to hsp70 sequences from other species. Expression experiments in Xenopus oocytes and mammalian cells indicate that a region that includes only 105 bp of 5' nontranscribed sequence contains all elements required for the efficient heat-controlled expression of the human gene. Two adjacent identical sequence elements, which are partly homologous to the Drosophila "heat shock consensus" sequence, are located 57 to 76 bp upstream from the capping site. Interestingly, the capping site itself is flanked by inverted repeat sequences.
Amin,
The heat shock consensus sequence is not sufficient for hsp70 gene expression in Drosophila melanogaster.
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The heat shock consensus sequence is not sufficient for hsp70 gene expression in Drosophila melanogaster.
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Drosophila gene related to the major heat shock-induced gene is transcribed at normal temperatures and not induced by heat shock.
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Regulation of heat-shock genes: a DNA sequence upstream of Drosophila hsp70 genes is essential for their induction in monkey cells.
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Induction of the synthesis of a 70,000 dalton mammalian heat shock protein by the adenovirus E1A gene product.
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A Drosophila RNA polymerase II transcription factor binds to the regulatory site of an hsp 70 gene.
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