Chaperone-like Activity

AAA nucleotidases share the common property of altering the conformation or association state of proteins, so it is not surprising that the RC has been shown to prevent aggregation of several denatured proteins including citrate synthase and ribonuclease A [59-61]. The chaperone activity of the RC may explain why the RC plays a role in transcription apparently in the absence of an attached 20S proteasome [62]. 

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Braun, B. C. et al. The base of the proteasome regulatory particle exhibits chaperone-like activity. Nat Cell Biol 1999, 3, 221-6. 

Braun, B.C., Glickman, M., KrtAFT, R., Dahlmann, B., Kloetzel, P.M., Finley, D., Schmidt, M., The base of the proteasome regulatory particle eidiibits chaperone-like activity. Nat. Cdl Biol. 1999, 1, 221-226. 

Akiyoshi K., Sasaki Y., Sunamoto J. Molecular chaperone-like activity of hydrogel nanoparticles of hydrophobized pullulan thermal stabilization with refolding of carbonic anhydrase B. Bioconjugates Chem. 1999 10(3) 321— 324. 

GUSTAVSSON, N., KOKKE, B.P., HARNDAHL, U., SILOW, M., BECHTOLD, U., POGHOSYAN, Z., MURPHY, D., BOELENS, W.C., SUNDBY, C., A peptide methionine sulfoxide reductase highly expressed in photosynthetic tissue in Arabidopsis thaliana can protect the chaperone-like activity of a chloroplast-localized small heat shock protein., Plant J.. 2002, 29, 545-553. 

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