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Modular recognition and binding properties of human heat shock transcription factor

A partially purified preparation of in vivo activated human heat shock transcription factor (HSF) has been obtained from HeLa cells and its interaction with the heat shock response element (HSE) in the human Hsp70 gene promoter was investigated. A variety of DNA-protein binding studies including DNAse I protection, hydroxyl radical protection, and diethylpyrocarbonate interference analysis were used to investigate recognition of the HSE by human HSF. Direct contacts to bases within the 5 basepair recognition motif were detected and the overall pattern of binding was compared with the Drosophila results. Analysis of the high resolution protection patterns to extended HSE mutants indicates that HSF binding coincides with the location of the additional element motifs. Moreover, examination of the protection patterns from these constructs indicate that a proposed model for HSF binding is consistent with a model depicting HSF as a trimer.

Identiferoai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.60480
Date January 1991
CreatorsWagner, John, 1966-
PublisherMcGill University
Source SetsLibrary and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada
LanguageEnglish
Detected LanguageEnglish
TypeElectronic Thesis or Dissertation
Formatapplication/pdf
CoverageMaster of Science (Department of Biology.)
RightsAll items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated.
Relationalephsysno: 001260458, proquestno: AAIMM72038, Theses scanned by UMI/ProQuest.

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