Investigating Possible Roles and Interactions Between RAC and NAC in Protecting Against Different Types of Stress

Proteins are essential for life. A protein’s function in cells heavily depends on its shape. When a protein is first made from a ribosome, the protein factory in a cell, it is just a single chain that does not have any shape. Then, this chain of protein folds into certain structure—like knitting a pair of gloves with wool—to perform its function. To ensure the proper folding of proteins, cells have developed various quality control systems. One of the cell’s quality control mechanisms is the use of chaperones attached to the ribosome. These chaperones provide the proper folding environment to protein chains that are freshly made by ribosome. The Ribosome-associated complex (RAC) and Nascent polypeptide-associated complex (NAC) constitute the ribosome-associated chaperone complexes and are present in most cells from yeast to human cells. In this research, we have investigated the effect of various combinations of the RAC and NAC subunits in viability of yeast cells under different stress