Question

combine fxns of chaperones and proteasomes - not ATP-dependant at low temps (20 C), these things in PROKARYOTES acts as a chaperone,at high temps, act as a protease to to remove misfolded or unfolded proteins

Answer 1

Certain proteins in prokaryotes serve as chaperones at lower temperatures to assist in proper protein folding and act as proteases at higher temperatures to degrade misfolded or damaged proteins.

Step-by-step explanation:

In prokaryotes, certain proteins can function both as chaperones and proteases, depending on the thermal conditions. At low temperatures (around 20°C), these molecules act as chaperones, aiding in the proper folding of other proteins to prevent misfolded or aggregated proteins that can occur due to abnormal environmental conditions. Conversely, at high temperatures, the same molecules can act as proteases, targeting denatured or misfolded proteins for degradation. This dual functionality aids in maintaining cellular protein quality control, ensuring that proteins achieve and maintain their correct structure necessary for biological activity or are efficiently removed if damaged.