Ribosome-DnaK interactions in relation to protein folding.

@article{Ghosh2003RibosomeDnaKII,
  title={Ribosome-DnaK interactions in relation to protein folding.},
  author={Jaydip Ghosh and Arunima Basu and Saumen Pal and Saheli Chowdhuri and Arpita Bhattacharya and Debashis Pal and Dhruba K Chattoraj and Chanchal K. Dasgupta},
  journal={Molecular microbiology},
  year={2003},
  volume={48 6},
  pages={
          1679-92
        }
}
Bacterial ribosomes or their 50S subunit can refold many unfolded proteins. The folding activity resides in domain V of 23S RNA of the 50S subunit. Here we show that ribosomes can also refold a denatured chaperone, DnaK, in vitro, and the activity may apply in the folding of nascent DnaK polypeptides in vivo. The chaperone was unusual as the native protein associated with the 50S subunit stably with a 1:1 stoichiometry in vitro. The binding site of the native protein appears to be different… CONTINUE READING

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