Purification and properties of drosophila heat shock activator protein

Carl Wu, Susan Wilson, Barbara Walker, Igor Dawid, Thomas Paisley, Vincenzo Zimarino, Hitoshi Ueda

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213 Citations (Scopus)

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 kiodaltons, 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.

Original languageEnglish
Pages (from-to)1247-1253
Number of pages7
JournalScience
Volume238
Issue number4831
DOIs
Publication statusPublished - Jan 1 1987
Externally publishedYes

ASJC Scopus subject areas

  • General

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    Wu, C., Wilson, S., Walker, B., Dawid, I., Paisley, T., Zimarino, V., & Ueda, H. (1987). Purification and properties of drosophila heat shock activator protein. Science, 238(4831), 1247-1253. https://doi.org/10.1126/science.3685975