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  The nucleotide exchange factors of Hsp70 molecular chaperones.

Bracher, A., & Verghese, J. (2015). The nucleotide exchange factors of Hsp70 molecular chaperones. Frontiers in molecular biosciences, 2: 10, pp. 1-9. doi:10.3389/fmolb.2015.00010.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-3ADF-9 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-3AE0-3
Genre: Journal Article

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 Creators:
Bracher, Andreas1, Author              
Verghese, Jacob1, Author              
Affiliations:
1Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              

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Free keywords: BAG domain; GrpE; Hsp110/Grp170; HspBP1/Sil1; cochaperone; protein folding; proteostasis
 Abstract: Molecular chaperones of the Hsp70 family form an important hub in the cellular protein folding networks in bacteria and eukaryotes, connecting translation with the downstream machineries of protein folding and degradation. The Hsp70 folding cycle is driven by two types of cochaperones: J-domain proteins stimulate ATP hydrolysis by Hsp70, while nucleotide exchange factors (NEFs) promote replacement of Hsp70-bound ADP with ATP. Bacteria and organelles of bacterial origin have only one known NEF type for Hsp70, GrpE. In contrast, a large diversity of Hsp70 NEFs has been discovered in the eukaryotic cell. These NEFs belong to the Hsp110/Grp170, HspBP1/Sil1, and BAG domain protein families. In this short review we compare the structures and molecular mechanisms of nucleotide exchange factors for Hsp70 and discuss how these cochaperones contribute to protein folding and quality control in the cell.

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Language(s): eng - English
 Dates: 2015
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: ISI: 26913285
DOI: 10.3389/fmolb.2015.00010
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Title: Frontiers in molecular biosciences
Source Genre: Journal
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Publ. Info: Lausanne : Frontiers
Pages: - Volume / Issue: 2 Sequence Number: 10 Start / End Page: 1 - 9 Identifier: ISSN: 2296-889X