Processing of proteins by the molecular chaperone Hsp104.

@article{Schaupp2007ProcessingOP,
  title={Processing of proteins by the molecular chaperone Hsp104.},
  author={Andreas Schaupp and Moritz Marcinowski and Valerie Grimminger and Benjamin B{\"o}sl and Stefan G Walter},
  journal={Journal of molecular biology},
  year={2007},
  volume={370 4},
  pages={674-86}
}
The molecular chaperone Hsp104 is an AAA+ ATPase (ATPase associated with a variety of cellular activities) from yeast that catalyzes protein disaggregation. Using mutagenesis, we impaired nucleotide binding or hydrolysis in the two nucleotide-binding domains (NBD) of Hsp104 and analyzed the consequences for chaperone function by monitoring ATP hydrolysis, polypeptide binding, polypeptide processing, and disaggregation. Our results reveal that ATP binding to NBD1 serves as a central regulatory… CONTINUE READING

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