Molecular chaperones are diverse families of multidomain proteins that have evolved to
assist nascent proteins to reach their native fold, protect subunits from heat shock during the …

Protein quality control within the cell requires the interplay of many molecular chaperones
and proteases. When this quality control system is disrupted, polypeptides follow pathways …

Abstract Bacterial ClpB and yeast Hsp104 are homologous Hsp100 protein disaggregases
that serve critical functions in proteostasis by solubilizing protein aggregates. Two AAA+ …

High-temperature stress can disrupt cellular proteostasis, resulting in the accumulation of
insoluble protein aggregates. For survival under stressful conditions, it is important for cells …

Hsp104 is a dynamic ring translocase and hexameric AAA+ protein found in yeast, which
couples ATP hydrolysis to disassembly and reactivation of proteins trapped in soluble …

Although the main players of the strigolactone (SL) signaling pathway have been
characterized genetically, how they regulate plant development is still poorly understood. Of …

Severe heat stress causes massive loss of essential proteins by aggregation, necessitating
a cellular activity that rescues aggregated proteins. This activity is executed by ATP …

The ClpB–DnaK bichaperone system reactivates aggregated cellular proteins and is
essential for survival of bacteria, fungi, protozoa, and plants under stress. AAA+ ATPase …

The oligomeric AAA+ chaperones Hsp104 in yeast and ClpB in bacteria are responsible for
the reactivation of aggregated proteins, an activity essential for cell survival during severe …

Rickettsiale diseases, including human monocytic ehrlichiosis caused by Ehrlichia
chaffeensis, are the second leading cause of the tick-borne infections in the USA and a …