ATP Hydrolysis Is Required for the DnaJ-dependent Activation of DnaK Chaperone for Binding to Both Native and Denatured Protein Substrates
Open Access
- 1 August 1995
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 270 (33), 19307-19311
- https://doi.org/10.1074/jbc.270.33.19307
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- The DnaJ chaperone catalytically activates the DnaK chaperone to preferentially bind the sigma 32 heat shock transcriptional regulator.Proceedings of the National Academy of Sciences, 1995
- A role for a eukaryotic GrpE-related protein, Mge1p, in protein translocation.Proceedings of the National Academy of Sciences, 1994
- DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70Trends in Biochemical Sciences, 1994
- Autoregulation of the Escherichia coli heat shock response by the DnaK and DnaJ heat shock proteins.Proceedings of the National Academy of Sciences, 1993
- Heat shock of Escherichia coli increases binding of dnaK (the hsp70 homolog) to polypeptides by promoting its phosphorylation.Proceedings of the National Academy of Sciences, 1993
- Initiation of lambda DNA replication. The Escherichia coli small heat shock proteins, DnaJ and GrpE, increase DnaK's affinity for the lambda P protein.Journal of Biological Chemistry, 1993
- Activity of the Hsp70 chaperone complex--DnaK, DnaJ, and GrpE--in initiating phage lambda DNA replication by sequestering and releasing lambda P protein.Proceedings of the National Academy of Sciences, 1992
- Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein foldingNature, 1992
- The DnaK chaperone modulates the heat shock response of Escherichia coli by binding to the sigma 32 transcription factor.Proceedings of the National Academy of Sciences, 1992
- Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK.Proceedings of the National Academy of Sciences, 1991