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  DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70

Cyr, D. M., Langer, T., & Douglas, M. G. (1994). DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70. Trends Biochem Sci, 19(4), 176-81.

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Item Permalink: https://hdl.handle.net/21.11116/0000-000B-6FCC-4 Version Permalink: https://hdl.handle.net/21.11116/0000-000B-6FCD-3
Genre: Journal Article

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https://www.ncbi.nlm.nih.gov/pubmed/8016869 (Any fulltext)
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 Creators:
Cyr, D. M., Author
Langer, T.1, Author           
Douglas, M. G., Author
Affiliations:
1Department Langer - Mitochondrial Proteostasis, Max Planck Institute for Biology of Ageing, Max Planck Society, ou_3393994              

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Free keywords: Escherichia coli/chemistry Escherichia coli Proteins Fungal Proteins/metabolism HSP40 Heat-Shock Proteins Heat-Shock Proteins/*metabolism Membrane Proteins/metabolism *Membrane Transport Proteins Mitochondria/metabolism Protein Folding Saccharomyces cerevisiae/chemistry *Saccharomyces cerevisiae Proteins
 Abstract: The folding of proteins and the assembly of protein complexes within subcompartments of the eukaryotic cell is catalysed by different members of the Hsp70 protein family. The chaperone function of Hsp70 proteins in these events is regulated by members of the DnaJ-like protein family, which occurs through direct interaction of different Hsp70 and DnaJ-like protein pairs that appear to be specifically adapted to each other. This review highlights the diversity of functions of DnaJ-like proteins by using specific examples of DnaJ-Hsp70 interactions with polypeptides in yeast protein-biogenesis pathways.

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 Dates: 1994-041994-04-01
 Publication Status: Issued
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 Identifiers: Other: 8016869
ISSN: 0968-0004 (Print)0968-0004 (Linking)
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Title: Trends Biochem Sci
Source Genre: Journal
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Pages: - Volume / Issue: 19 (4) Sequence Number: - Start / End Page: 176 - 81 Identifier: -