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 …

Publisher Summary The mechanisms underlying ethanol and heat tolerance are complex.
The integrity of cytoplasmic and mitochondrial membranes is critical to maintain proton …

Hsp104 is a stress tolerance factor that promotes the reactivation of heat-damaged proteins
in yeast by an unknown mechanism. Herein, we demonstrate that Hsp104 functions in this …

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

ClpB of Escherichia coli is an ATP-dependent ring-forming chaperone that mediates the
resolubilization of aggregated proteins in cooperation with the DnaK chaperone system …

The bacterial DnaA protein binds to the chromosomal origin of replication to trigger a series
of initiation reactions, which leads to the loading of DNA polymerase III. In Escherichia coli …

Hsp101 is a molecular chaperone that is required for the development of thermotolerance in
plants and other organisms. We report that Arabidopsis thaliana Hsp101 is also regulated …

In the yeast Saccharomyces cerevisiae, Sup35p (eRF3), a subunit of the translation
termination complex, can take up a prion‐like, self‐propagating conformation giving rise to …

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 …

Mutations in the AAA adenosine triphosphatase (ATPase) Spastin (SPG4) cause an
autosomal dominant form of hereditary spastic paraplegia, which is a retrograde axonopathy …