▪ Abstract Ribulose-1, 5-bisphosphate (RuBP) carboxylase/oxygenase (Rubisco) catalyzes
the first step in net photosynthetic CO2 assimilation and photorespiratory carbon oxidation …

Members of the diverse superfamily of AAA+ proteins are molecular machines responsible
for a wide range of essential cellular processes. In this review we summarise structural and …

Unicellular and sessile organisms are particularly exposed to environmental stress such as
heat shock causing accumulation and aggregation of misfolded protein species. To …

It is not understood how Hsp104, a hexameric AAA+ ATPase from yeast, disaggregates
diverse structures, including stress-induced aggregates, prions, and α-synuclein conformers …

In vivo function of the molecular chaperone Hsp90 is ATP-dependent and requires the full-
length protein. Our earlier studies predicted a second C-terminal ATP-binding site in Hsp90 …

Saccharomyces cerevisiae Hsp104, a hexameric member of the Hsp100/Clp subfamily of
AAA+ ATPases with two nucleotide binding domains (NBD1 and 2), refolds aggregated …

In vivo propagation of [PSI+], an aggregation-prone prion isoform of the yeast release factor
Sup35 (eRF3), has previously been shown to require intermediate levels of the chaperone …

At the Cold Spring Harbor Meeting on 'Molecular Chaperones and the Heat Shock
Response'in May 1996, Susan Lindquist presented evidence that a chaperone of yeast …

AAA proteins share a conserved active site for ATP hydrolysis and regulate many cellular
processes. AAA proteins are oligomeric and often have multiple ATPase domains per …

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 …