ArticleProceedings of the National Academy of Sciences of the United States of America2002
The substrate binding domain of DnaK facilitates slow protein refolding.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Rapid screening of high expressing Escherichia coli colonies using a novel dicistronic-autoinducible system.Microbial cell factories · 2021Article
- Comparison of E. coli based self-inducible expression systems containing different human heat shock proteins.Scientific reports · 2021Article
- Cytosolic Hsp70 and co-chaperones constitute a novel system for tRNA import into the nucleus.eLife · 2015Article
- Mutagenesis reveals the complex relationships between ATPase rate and the chaperone activities of Escherichia coli heat shock protein 70 (Hsp70/DnaK).The Journal of biological chemistry · 2010Article
- Comparing the functional properties of the Hsp70 chaperones, DnaK and BiP.Biophysical chemistry · 2010Article
- Ternary system of solution additives with arginine and salt for refolding of beta-galactosidase.The protein journal · 2010Article
- Interaction of the N-terminal domain of Escherichia coli heat-shock protein ClpB and protein aggregates during chaperone activity.Protein science : a publication of the Protein Society · 2004Article
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6 authors.
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Abstract
We examined the effects of a fragment of the substrate binding domain of DnaK on protein refolding from chemically denatured states. The fragment DnaK384-638, containing a full-length substrate binding domain, tightly binds to the unfolded protein in solution. The effects of DnaK384-638 on the reactivation of beta-galactosidase and luciferase were examined at low substrate concentration and low temperature, conditions in which the folding is significantly slow (several days) but the reactivation yield is higher than those in ordinary refolding conditions. In the presence of DnaK384-638, the maximum yield of active beta-galactosidase was improved from 45% to 65% after a 48-h refolding reaction. Spectroscopic experiments showed that DnaK384-638 bound to partially structured monomers of beta-galactosidase and consequently suppressed aggregation. DnaK384-638 accelerated the refolding of luciferase to attain equilibrium in 8 h. On the other hand, DnaK386-561, which has no affinity for the substrate, had no chaperone activity for the reactivation of these proteins. These results indicate that the substrate binding of DnaK384-638 facilitates slow protein refolding.
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