The small heat shock protein Hsp42 controls the spatio-temporal organization of aggregated proteins in Saccharomyces cerevisiae [Elektronische Ressource] / presented by Sebastian Specht


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INAUGURAL-DISSERTATION submitted to the Combined Faculties for the Natural Sciences and for Mathematics of the Ruperto-Carola University of Heidelberg, Germany for the degree of Doctor of Natural Sciences presented by M.Sc. Sebastian Specht born in Berlin Oral examination: 22 July 2010 The Small Heat Shock Protein Hsp42 Controls The Spatio-Temporal Organization Of Aggregated Proteins In Saccharomyces Cerevisiae Referees: 1. Prof. Dr. Bernd Bukau 2. Prof. Dr. Elmar Schiebel Summary Summary Stress-induced protein aggregation represents a major threat for cell survival and is also associated with various human disorders and cellular aging. The primary cellular response to aberrant protein conformations is the refolding of misfolded proteins by molecular chaperones or their elimination by AAA+ proteases. Once this first line of defense has been overrun, aggregated proteins are directed to specific compartments, thus protecting the cellular environment from potentially deleterious protein conformations. Organizing protein aggregates might also facilitate the recruitment of protein quality control components, thereby increasing the efficiency of aggregate removal in a subsequent phase.



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Published 01 January 2010
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Language English
Document size 23 MB
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