Interaction of oxidized chaperonin GroEL with an unfolded protein at low temperatures.

Academic Article


  • The chaperonin GroEL binds to non-native substrate proteins via hydrophobic interactions, preventing their aggregation, which is minimized at low temperatures. In the present study, we investigated the refolding of urea-denatured rhodanese at low temperatures, in the presence of ox-GroEL (oxidized GroEL), which contains increased exposed hydrophobic surfaces and retains its ability to hydrolyse ATP. We found that ox-GroEL could efficiently bind the urea-unfolded rhodanese at 4°C, without requiring excess amount of chaperonin relative to normal GroEL (i.e. non-oxidized). The release/reactivation of rhodanese from GroEL was minimal at 4°C, but was found to be optimal between 22 and 37°C. It was found that the loss of the ATPase activity of ox-GroEL at 4°C prevented the release of rhodanese from the GroEL-rhodanese complex. Thus ox-GroEL has the potential to efficiently trap recombinant or non-native proteins at 4°C and release them at higher temperatures under appropriate conditions.
  • Authors


  • Animals, Cattle, Chaperonin 60, Cold Temperature, Kinetics, Liver, Oxidation-Reduction, Protein Binding, Protein Denaturation, Protein Refolding, Thiosulfate Sulfurtransferase, Urea
  • Digital Object Identifier (doi)

    Author List

  • Melkani GC; Sielaff R; Zardeneta G; Mendoza JA
  • Start Page

  • 299
  • End Page

  • 303
  • Volume

  • 32
  • Issue

  • 3