Abstract
Drosophila heat shock activator protein, a rare transacting factor which is induced upon heat shock to bind specifically to the heat shock regulatory sequence in vivo, has been purified from shocked cells to more than 95 percent homogeneity by sequence-specific duplex oligonucleotide affinity chromatography. The purified protein has a relative molecular mass of 110 kilodaltons, binds to the regulatory sequence with great affinity and specificity, and strongly stimulates transcription of the Drosophila hsp70 gene. Studies with this regulatory protein should lead to an understanding of the biochemical pathway underlying the heat shock phenomenon.
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Dates
Type | When |
---|---|
Created | 18 years, 10 months ago (Oct. 5, 2006, 4:28 p.m.) |
Deposited | 1 year, 7 months ago (Jan. 14, 2024, 5:21 a.m.) |
Indexed | 11 months, 2 weeks ago (Sept. 11, 2024, 1:53 a.m.) |
Issued | 37 years, 9 months ago (Nov. 27, 1987) |
Published | 37 years, 9 months ago (Nov. 27, 1987) |
Published Print | 37 years, 9 months ago (Nov. 27, 1987) |
@article{Wu_1987, title={Purification and Properties of Drosophila Heat Shock Activator Protein}, volume={238}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.3685975}, DOI={10.1126/science.3685975}, number={4831}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Wu, Carl and Wilson, Susan and Walker, Barbara and Dawid, Igor and Paisley, Thomas and Zimarino, Vincenzo and Ueda, Hitoshi}, year={1987}, month=nov, pages={1247–1253} }