Study of the yeast cytosolic Hsp70-system in protein homeostasis and life span regulation - The misfolding protein marker guk1-7-GFP before, during and after in recovery from heat shock stress in Hsp70-mutant yeast strains

Our study aims to answer the question "Which functions of the Hsp70 class of molecular chaperones are essential for yeast to maintain a standard replicative life span?". To answer this question, we utilised the disparate functions of the Hsp70's Ssa1 and 2 and their paralog Ssa4 in a yeast strain that lacks Ssa1/2 but has an ectopically increased production of Ssa4. We have gathered data on the behaviour of several different markers for protein aggregation under different circumstances, as well as data on proteins from other classes of molecular chaperones. The bulk of the data is in the form of multichannel microscopy images from widefield microscopy, with a few sets of western blots of protein extracts. Fluorescence microscopy of live yeast cells at mid-exponential growth before stress, directly after 30 minutes of heat shock, and 20, 40 and 60 minutes after heat shock. The yeast is grown in complete synthetic medium with 2 % glucose as carbon source. All strains produce the aggregate marker protein guk1-7-GFP. The dataset was collected through fluorescence microscopy. The image files are provided in Carl Zeiss Image format (.czi).