The Hsc66-Hsc20 chaperone system in Escherichia coli: chaperone activity and interactions with the DnaK-DnaJ-grpE system.

@article{Silberg1998TheHC,
  title={The Hsc66-Hsc20 chaperone system in Escherichia coli: chaperone activity and interactions with the DnaK-DnaJ-grpE system.},
  author={J. Silberg and K. Hoff and L. Vickery},
  journal={Journal of bacteriology},
  year={1998},
  volume={180 24},
  pages={
          6617-24
        }
}
  • J. Silberg, K. Hoff, L. Vickery
  • Published 1998
  • Biology, Medicine
  • Journal of bacteriology
  • Hsc66, a stress-70 protein, and Hsc20, a J-type accessory protein, comprise a newly described Hsp70-type chaperone system in addition to DnaK-DnaJ-GrpE in Escherichia coli. Because endogenous substrates for the Hsc66-Hsc20 system have not yet been identified, we investigated chaperone-like activities of Hsc66 and Hsc20 by their ability to suppress aggregation of denatured model substrate proteins, such as rhodanese, citrate synthase, and luciferase. Hsc66 suppressed aggregation of rhodanese and… CONTINUE READING
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