Question

A descrptive pathway of Heat Shock Protein 104 and A pathway of the Gene knockout in yeast. ( on a biological level )

Answer 1

Cells produce optimally within a relatively fine temperature range but tolerate modest deviations, some of which impose upon cell structure and function, via fast physiological adaptations. The adaptation mechanisms is the heat shock response (HSR), a highly preserved program of changes in gene expression that result in the repression of the protein biosynthetic capacity and the induction of a battery of cytoprotective genes encoding the heat shock proteins (HSPs). Different HSPs function as molecular chaperones to strongly protect thermally damaged proteins from unfold aggregated proteins, aggregation and refold damaged proteins or target them for efficient degradation. Physiological alterations such as the synthesis of compatible solutes, cell wall, and the transient break of the cell cycle also contribute to cellular survival. The HSR in eukaryotic cells has been clarified with the model yeast Saccharomyces cerevisiae due to its glib of, biochemistry, genetics and cell biology as well as the wealth of genome-level tools made available.The Hsp104 protein chaperone and works synergistically with trehalose to stabilize the yeast proteome at high temperatures. Indeed, both trehalose and Hsp104 are required for tolerance to heat shock

The eukaryotic heat shock response transcriptional program that results in synthesis of a battery of cytoprotective genes in the attendance of environmental and other thermal stresses. Many of these genes encode molecular chaperones, influential protein remodelers with the capacity to shield, fold, or unfold substrates in a context-dependent manner. The Saccharomyces cerevisiae budding yeast stays to be an model for driving the regulatory features of different stress response. The budding yeast has been an model system to explain the cell biology of protein chaperones and their organization into purposeful networks.