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  Action of the Hsp70 chaperone system observed with single proteins

Nunes, J. M., Mayer-Hartl, M., Hartl, F. U., & Mueller, D. J. (2015). Action of the Hsp70 chaperone system observed with single proteins. NATURE COMMUNICATIONS, 6, 6307-6307. doi:10.1038/ncomms7307.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0026-A77D-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0026-A77E-B
Genre: Journal Article

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 Creators:
Nunes, Joao M.1, Author
Mayer-Hartl, Manajit2, Author              
Hartl, F. Ulrich3, Author              
Mueller, Daniel J.1, Author
Affiliations:
1external, ou_persistent22              
2Hayer-Hartl, Manajit / Chaperonin-assisted Protein Folding, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565153              
3Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              

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 Abstract: In Escherichia coli, the binding of non-native protein substrates to the Hsp70 chaperone DnaK is mediated by the co-chaperone DnaJ. DnaJ accelerates ATP hydrolysis on DnaK, by closing the peptide-binding cleft of DnaK. GrpE catalysed nucleotide exchange and ATP re-binding then lead to substrate release from DnaK, allowing folding. Here we refold immunoglobulin 27 (I27) to better understand how DnaJ-DnaK-GrpE chaperones cooperate. When DnaJ is present, I27 is less likely to misfold and more likely to fold, whereas the unfolded state remains unaffected. Thus, the 'holdase' DnaJ shows foldase behaviour. Misfolding of I27 is fully abrogated when DnaJ cooperates with DnaK, which stabilizes the unfolded state and increases the probability of folding. Addition of GrpE shifts the unfolded fraction of I27 to pre-chaperone levels. These insights reveal synergistic mechanisms within the evolutionary highly conserved Hsp70 system that prevent substrates from misfolding and promote their productive transition to the native state.

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Language(s): eng - English
 Dates: 2015-02
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: ISI: 000350290300005
DOI: 10.1038/ncomms7307
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Title: NATURE COMMUNICATIONS
Source Genre: Journal
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Pages: - Volume / Issue: 6 Sequence Number: - Start / End Page: 6307 - 6307 Identifier: ISSN: 2041-1723