Processing of Proteins by the Molecular Chaperone Hsp104 Export

@article{citeulike:1378259, abstract = {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 switch for the chaperone; it triggers binding of polypeptides, and stimulates ATP hydrolysis in the C-terminal NBD2 by more than two orders of magnitude, implying that ATP hydrolysis in this domain is important for disaggregation. Moreover, we show that Hsp104 actively unfolds its polypeptide substrates during processing, demonstrating that AAA+ proteins involved in disaggregation share a common threading mechanism with AAA+ proteins mediating protein unfolding/degradation.}, author = {Schaupp, Andreas and Marcinowski, Moritz and Grimminger, Valerie and Bosl, Benjamin and Walter, Stefan}, citeulike-article-id = {1378259}, citeulike-linkout-0 = {http://www.sciencedirect.com/science/article/B6WK7-4NN6TRT-4/2/481149bcde7c01950b2f666d2e66e4f1}, day = {20}, journal = {Journal of Molecular Biology}, keywords = {chaperone, protein-degradation}, month = {July}, number = {4}, pages = {674--686}, posted-at = {2007-06-11 08:20:38}, priority = {2}, title = {Processing of Proteins by the Molecular Chaperone Hsp104}, url = {http://www.sciencedirect.com/science/article/B6WK7-4NN6TRT-4/2/481149bcde7c01950b2f666d2e66e4f1}, volume = {370}, year = {2007} }

TY - JOUR ID - citeulike:1378259 L3 - citeulike-article-id:1378259 N2 - 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 switch for the chaperone; it triggers binding of polypeptides, and stimulates ATP hydrolysis in the C-terminal NBD2 by more than two orders of magnitude, implying that ATP hydrolysis in this domain is important for disaggregation. Moreover, we show that Hsp104 actively unfolds its polypeptide substrates during processing, demonstrating that AAA+ proteins involved in disaggregation share a common threading mechanism with AAA+ proteins mediating protein unfolding/degradation. IS - 4 JF - Journal of Molecular Biology EP - 686 TI - Processing of Proteins by the Molecular Chaperone Hsp104 VL - 370 SP - 674 KW - chaperone KW - protein-degradation AU - Schaupp, Andreas AU - Marcinowski, Moritz AU - Grimminger, Valerie AU - Bosl, Benjamin AU - Walter, Stefan PY - 2007/07/20/ UR - http://www.sciencedirect.com/science/article/B6WK7-4NN6TRT-4/2/481149bcde7c01950b2f666d2e66e4f1 ER -