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- W91918504 abstract "The heat shock response presents an extremely attractive model to study the regulation of gene transcription in eucaryotes. I have focused the bulk of my researchefforts on investigating the molecular determinants of protein-DNA interaction exhibited by the heat-shock transcription factor (HSTF) of Drosophila. The specificcontacts made by the HSTF upon binding to the heat-shock element (HSE) were exhaustively determined using a variety of chemical and enzymatic probes for a number of HSTF-HSE complexes formed at both hsp70 and hsp83 gene promoters.During the course of these studies it is demonstrated that the HSTF appears to polymerize in a sequence-specific and template-directed manner on each of these promoters, a novelty in this class of regulators. Evidence suggesting that DNA bending may occur during this HSTF-DNA association on the hsp70 promoter is also presented. This observation represented the first report of a eucaryotic transcriptionalactivator exhibiting this property. Significantly, during the course of these studies two novel technologies were advanced; namely the gel-based contact point method and sequence-specific DNA affinity purification methodology. These technical advancements and the HSTF-HSE interaction results will be discussed in the body of the thesis in light of their relevance to both heat-shock and global gene expression mechanisms." @default.
- W91918504 created "2016-06-24" @default.
- W91918504 creator A5045962198 @default.
- W91918504 date "2002-01-01" @default.
- W91918504 modified "2023-09-23" @default.
- W91918504 title "A detailed analysis of the DNA binding properties and the affinity purification of the Drosophila heat-shock transcription factor" @default.
- W91918504 hasPublicationYear "2002" @default.
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