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Science 27 November 1987:
Vol. 238. no. 4831, pp. 1247 - 1253
DOI: 10.1126/science.3685975
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Articles

Science, Vol 238, Issue 4831, 1247-1253
Copyright © 1987 by American Association for the Advancement of Science

articles

Purification and properties of Drosophila heat shock activator protein

C Wu, S Wilson, B Walker, I Dawid, T Paisley, V Zimarino, and H Ueda

Laboratory of Biochemistry, National Cancer Institute, Bethesda, MD 20892.

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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Science. ISSN 0036-8075 (print), 1095-9203 (online)