Dual Function of Protein Confinement in Chaperonin-Assisted Protein Folding

@article{Brinker2001DualFO,
  title={Dual Function of Protein Confinement in Chaperonin-Assisted Protein Folding},
  author={Achim Brinker and G{\"u}nther W. Pfeifer and Michael J. Kerner and Dean J. Naylor and F. Ulrich Hartl and Manajit Hayer-Hartl},
  journal={Cell},
  year={2001},
  volume={107},
  pages={223-233}
}
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… CONTINUE READING