Ontology highlight
ABSTRACT:
SUBMITTER: Gates SN
PROVIDER: S-EPMC5770238 | biostudies-literature | 2017 Jul
REPOSITORIES: biostudies-literature
Gates Stephanie N SN Yokom Adam L AL Lin JiaBei J Jackrel Meredith E ME Rizo Alexandrea N AN Kendsersky Nathan M NM Buell Courtney E CE Sweeny Elizabeth A EA Mack Korrie L KL Chuang Edward E Torrente Mariana P MP Su Min M Shorter James J Southworth Daniel R DR
Science (New York, N.Y.) 20170615 6348
Hsp100 polypeptide translocases are conserved members of the AAA+ family (adenosine triphosphatases associated with diverse cellular activities) that maintain proteostasis by unfolding aberrant and toxic proteins for refolding or proteolytic degradation. The Hsp104 disaggregase from <i>Saccharomyces cerevisiae</i> solubilizes stress-induced amorphous aggregates and amyloids. The structural basis for substrate recognition and translocation is unknown. Using a model substrate (casein), we report c ...[more]