Thesis (Ph. D.)--University of Texas at Austin, 2003. / Vita. Includes bibliographical references. Available also from UMI Company.

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.

Thesis (M.Med.Sc.)--University of Hong Kong, 2008. / Includes bibliographical references (p. 53-65)

Thesis (Ph. D.)--University of Washington, 2004. / Vita. Includes bibliographical references (leaves 151-162).

Thesis (M. Phil.)--University of Hong Kong, 2005. / Title proper from title frame. Also available in printed format.

Thesis (Ph. D.)--University of Wisconsin--Madison, 1968. / Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliography.

The study focuses on the effects of heat stress on <i>Serpula lacrymans</i> and <i>S. himantioides</i> (which have been previously shown to be relatively thermosensitive and thermotolerant respectively) in relation to the heat shock response. A part of this response is the production of heat-shock proteins (hsps). Comparative studies of chick embryo fibroblasts and <i>Saccharomyces cerevisiae</i> (wine strain, L-2226) were used to demonstrate possible differences between these three very distinct eukaryotic systems. The aims of the project were to determine whether <i>S. lacrymans</i> and <i>S. himantioides</i> undergo the heatshock response with respect primarily to induced thermotolerance and the production of hsps. The approach taken to establish the above was by systematic analysis of the different pathways involved in this response. Firstly, overall heat induced changes in protein and mRNA synthesis were analysed, in conjunction with the identification of specific proteins related to the heat-shock response, namely hsp60, hsp70 which have been shown in other eukaryotic systems to play key roles in this response. Secondly, immunological studies were also used to detect changes in the pattern of protein ubiquitination, which resulted from heat stress. Thirdly, changes in hsp70 mRNA were monitored by RT-PCR. The cDNA and genomic amplimer products generated by RT-PCR and PCR respectively were cloned and sequenced to identify a putative of hsp70 gene sequence. Fourthly, the AMP-activated protein kinase (AMPK) cascade has been demonstrated to be activated in response to stress and steps were made to detect and identify AMPK activity in cellular extracts of both <i>Serpula </i>species. Finally, the effect of heat upon trehalose accumulation and mobilisation during the heat-shock response was studied as there is growing evidence to link increased thermotolerance to transient increase in trehalose levels, which is now considered to be a stress metabolite.

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