[HTML][HTML] Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery
S Diamant, AP Ben-Zvi, B Bukau… - Journal of Biological …, 2000 - ASBMB
Classic in vitro studies show that the Hsp70 chaperone system from Escherichia coli (DnaK-
DnaJ-GrpE, the DnaK system) can bind to proteins, prevent aggregation, and promote the
correct refolding of chaperone-bound polypeptides into native proteins. However, little is
known about how the DnaK system handles proteins that have already aggregated. In this
study, glucose-6-phosphate dehydrogenase was used as a model system to generate stable
populations of protein aggregates comprising controlled ranges of particle sizes. The DnaK …
DnaJ-GrpE, the DnaK system) can bind to proteins, prevent aggregation, and promote the
correct refolding of chaperone-bound polypeptides into native proteins. However, little is
known about how the DnaK system handles proteins that have already aggregated. In this
study, glucose-6-phosphate dehydrogenase was used as a model system to generate stable
populations of protein aggregates comprising controlled ranges of particle sizes. The DnaK …