Publication Date:
1987-11-27
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wu, C -- Wilson, S -- Walker, B -- Dawid, I -- Paisley, T -- Zimarino, V -- Ueda, H -- New York, N.Y. -- Science. 1987 Nov 27;238(4831):1247-53.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Biochemistry, National Cancer Institute, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3685975" target="_blank"〉PubMed〈/a〉
Keywords:
Animals
;
Base Sequence
;
Drosophila/*genetics
;
*Genes
;
*Genes, Regulator
;
Heat-Shock Proteins/*genetics
;
Kinetics
;
Molecular Weight
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
