Study of the yeast cytosolic Hsp70-system in protein homeostasis and life span regulation - Silver stained 2D-gels of protein extracts from wild type and 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. Images of two dimensional protein gels with protein extracts from wild type and Hsp70 mutant yeast strains in mid-exponential growth phase. The yeast were grown in rich medium (YP) with 2 % glucose as carbon source. The images have been aligned and the background has been removed. The dataset was collected through imaging of two dimensional protein gels. The image files are provided in TIFF format.
Andersson R, Eisele-Bürger AM, Hanzén S, Vielfort K, Öling D, Eisele F, Johansson G, Gustafsson T, Kvint K, Nyström T. Differential role of cytosolic Hsp70s in longevity assurance and protein quality control. bioRxiv. 2020 Jun 29. Available from: https://www.biorxiv.org/content/10.1101/2020.06.25.170670v2.full
Andersson R, Eisele-Bürger AM, Hanzén S, Vielfort K, Öling D, Eisele F, et al. (2021) Differential role of cytosolic Hsp70s in longevity assurance and protein quality control. PLoS Genet 17(1): e1008951.
Discovery Biology, Discovery Sciences, Innovative Medicines and Early Development Biotech Unit
Institute of Biomedicine, Department of Microbiology and Immunology
Process by which cells irreversibly stop dividing and enter a state of permanent growth arrest without undergoing CELL DEATH. Senescence can be induced by DNA DAMAGE or other cellular stresses, such as OXIDATIVE STRESS.
A family of cellular proteins that mediate the correct assembly or disassembly of polypeptides and their associated ligands. Although they take part in the assembly process, molecular chaperones are not components of the final structures.
A class of MOLECULAR CHAPERONES found in both prokaryotes and in several compartments of eukaryotic cells. These proteins can interact with polypeptides during a variety of assembly processes in such a way as to prevent the formation of nonfunctional structures.
Disorders caused by imbalances in the PROTEIN HOMEOSTASIS network - synthesis, folding, and transport of proteins; post-translational modifications; and degradation or clearance of misfolded proteins.
data/2d gel electrophoresis/2D gel electrophoresis.zip
documentation/2D gel electrophoresis.pdf
documentation/GFP-HSP104 in WT and HSP70 mutants.pdf
documentation/GFP-HSP104 in WT and ssa12DD with SSA1-4 chimaeras.pdf
documentation/guk1-7-GFP w Sik1-RFP and DAPI.pdf
documentation/guk1-7-GFP w-wo HSP104 microscopy.pdf
documentation/ReadMe Access to microscopy files.pdf
documentation/Ssa4-GFP Mca1-RFP microscopy.pdf
documentation/Total Hsp70 western blots.pdf