Question

Why would heat shock proteins be present at low levels in cells or organisms raised at normal temperatures and then increase in number after a brief exposure to elevated temperatures?

Answer 1

Heat shock proteins assist in the refolding of misfolded proteins, which can occur during elevated temperatures.

Step-by-step explanation:

Heat shock proteins (HSPs) function as molecular chaperones, assisting in the correct folding of proteins, particularly under stressful conditions such as elevated temperatures. At normal conditions, cells maintain a low level of HSPs as not all proteins require assistance in folding. However, during a heat shock, proteins may denature or misfold due to the stress of increased temperatures. In this scenario, cells respond by increasing the production and activation of HSPs to refold misfolded proteins and protect the cell from potential damage. This process involves the release of HSPs from the NR/HSP complex and the increased transcription of HSP genes, a protective mechanism that has evolved even though most cells do not typically encounter extreme heat conditions.

The role of HSP chaperones is to prevent protein aggregation during folding and assist with the correct conformation of proteins under both normal and stress conditions, supporting essential cellular functions and survival.