Final answer:
In response to misfolded proteins, the cell induces genes encoding heat shock proteins as part of the unfolded protein response to assist in refolding proteins and maintaining their functions. This mechanism is crucial for cellular survival under stressful conditions, such as elevated temperatures, that can disrupt protein folding.
Step-by-step explanation:
In response to the accumulation of misfolded proteins, genes encoding heat shock proteins (HSP) are typically induced during the unfolded protein response (UPR). Heat shock proteins are important chaperones that assist in refolding misfolded proteins. This is vital because the proper folding of proteins is crucial for their function. Misfolded proteins can result in loss of function or gain of toxic function, leading to proteopathies such as Alzheimer's and Creutzfeldt-Jakob disease.
In conditions of stress such as increased temperature, cells increase the activity of heat shock proteins to maintain protein stability and prevent aggregation, ensuring cellular proteins retain or regain their functional three-dimensional structures.
When a cell experiences a 'heat shock' or increased temperatures, the heat shock proteins are activated by release from the NR/HSP complex, and the transcription of HSP genes is also activated. This response is critical, as abnormal conditions such as high temperature or extreme pH levels can prevent proteins from folding correctly. By enhancing the activity of heat shock proteins, the cell has a better chance of surviving stressful conditions by stabilizing and refolding damaged proteins.