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  Dual Function of Protein Confinement in Chaperonin-assisted Protein Folding

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-7134-0 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-7135-E
Genre: Journal Article

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Brinker, A.1, Author              
Pfeifer, G.1, Author              
Kerner, M.J., Author
Naylor, D.J., Author
Hartl, F. U.1, Author              
Hayer-Hartl, M. K.1, Author              
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1External Organizations, ou_persistent22              

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 Abstract: 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.

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 Dates: 2001
 Publication Status: Published in print
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 Identifiers: eDoc: 318527
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Title: Cell
Source Genre: Journal
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Pages: - Volume / Issue: 107 (2) Sequence Number: - Start / End Page: 223 - 233 Identifier: -