Question

Combine functions of chaperones and proteasomes. Not ATP-dependent. At low temps (20°C), these things in PROKARYOTES act as a chaperone, at high temps, act as a protease to remove misfolded or unfolded proteins.

A) ClpP
B) Lon protease
C) GroEL
D) Hsp70

Answer 1

Chaperones and proteasomes in prokaryotes have different roles depending on the temperature. Chaperones assist in protein folding at low temperatures, while proteasomes degrade misfolded proteins at high temperatures.

Step-by-step explanation:

Chaperones and proteasomes are two important components involved in protein folding and degradation in prokaryotes. Chaperones help properly fold proteins and prevent their aggregation at low temperatures, while proteasomes act as proteases to remove misfolded or unfolded proteins at high temperatures. A common example of a chaperone is GroEL, which assists in protein folding. Hsp70 is another chaperone that aids in protein folding and transport across membranes. ClpP and Lon protease are examples of proteasomes that degrade misfolded proteins.