Help Privacy Policy Disclaimer
  Advanced SearchBrowse




Journal Article

Dual Function of Protein Confinement in Chaperonin-assisted Protein Folding

There are no MPG-Authors in the publication available
External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available

Brinker, A., Pfeifer, G., Kerner, M., Naylor, D., Hartl, F. U., & Hayer-Hartl, M. K. (2001). Dual Function of Protein Confinement in Chaperonin-assisted Protein Folding. Cell, 107(2), 223-233.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-7134-0
The GroEL/GroES chaperonin system mediates the folding of a range of newly synthesized polypeptides in the bacterial cytosol. Using a rapid biotin-streptavidin-based inhibition of chaperonin function, we show that the cage formed by GroEL and its cofactor GroES can have a dual role in promoting folding. First, enclosure of nonnative protein in the GroEL:GroES complex is essential for folding to proceed unimpaired by aggregation. Second, folding inside the cage can be significantly faster than folding in free solution, independently of ATP-driven cycles of GroES binding and release. This suggests that confinement of unfolded protein in the narrow hydrophilic space of the chaperonin cage smoothes the energy landscape for the folding of some proteins, increasing the flux of folding intermediates toward the native state.