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  GroEL/ES Chaperonin Modulates the Mechanism and Accelerates the Rate of TIM-Barrel Domain Folding

Georgescauld, F., Popova, K., Gupta, A. J., Bracher, A., Engen, J. R., Hayer-Hartl, M., et al. (2014). GroEL/ES Chaperonin Modulates the Mechanism and Accelerates the Rate of TIM-Barrel Domain Folding. CELL, 157(4), 922-934. doi:10.1016/j.cell.2014.03.038.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-CE2F-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-CE30-6
Genre: Journal Article

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 Creators:
Georgescauld, Florian1, Author              
Popova, Kristina1, Author              
Gupta, Amit J.1, Author              
Bracher, Andreas1, Author              
Engen, John R.2, Author
Hayer-Hartl, Manajit3, Author              
Hartl, F. Ulrich1, Author              
Affiliations:
1Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              
2external, ou_persistent22              
3Hayer-Hartl, Manajit / Chaperonin-assisted Protein Folding, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565153              

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Free keywords: MASS-SPECTROMETRY; HYDROGEN-EXCHANGE; ESCHERICHIA-COLI; IN-VIVO; E. COLI; PROTEIN; CONFINEMENT; RESOLUTION; KINETICS; MODEL
 Abstract: The GroEL/ES chaperonin system functions as a protein folding cage. Many obligate substrates of GroEL share the (beta alpha)(8) TIM-barrel fold, but how the chaperonin promotes folding of these proteins is not known. Here, we analyzed the folding of DapA at peptide resolution using hydrogen/deuterium exchange and mass spectrometry. During spontaneous folding, all elements of the DapA TIM barrel acquire structure simultaneously in a process associated with a long search time. In contrast, GroEL/ES accelerates folding more than 30-fold by catalyzing segmental structure formation in the TIM barrel. Segmental structure formation is also observed during the fast spontaneous folding of a structural homolog of DapA from a bacterium that lacks GroEL/ES. Thus, chaperonin independence correlates with folding properties otherwise enforced by protein confinement in the GroEL/ES cage. We suggest that folding catalysis by GroEL/ES is required by a set of proteins to reach native state at a biologically relevant time scale, avoiding aggregation or degradation.

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Language(s): eng - English
 Dates: 2014
 Publication Status: Published in print
 Pages: 13
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Degree: -

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Title: CELL
Source Genre: Journal
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Publ. Info: 600 TECHNOLOGY SQUARE, 5TH FLOOR, CAMBRIDGE, MA 02139 USA : CELL PRESS
Pages: - Volume / Issue: 157 (4) Sequence Number: - Start / End Page: 922 - 934 Identifier: ISSN: 0092-8674