[HTML][HTML] The ATPase activity of Hsp104, effects of environmental conditions and mutations
EC Schirmer, C Queitsch, AS Kowal, DA Parsell… - Journal of Biological …, 1998 - ASBMB
Hsp104 is crucial for stress tolerance inSaccharomyces cerevisiae, and both of its
nucleotide-binding domains (NBD1 and NBD2) are required. Here, we characterize the
ATPase activity and oligomerization properties of wild-type (WT) Hsp104 and of NBD
mutants. In physiological ionic strength buffers (pH 7.5, 37° C) WT Hsp104 exhibits
Michaelis-Menten kinetics between 0.5 and 25 mm ATP (K m∼ 5 mm, V max∼ 2 nmol min−
1 μg− 1). ATPase activity is strongly influenced by factors that vary with cell stress (eg …
nucleotide-binding domains (NBD1 and NBD2) are required. Here, we characterize the
ATPase activity and oligomerization properties of wild-type (WT) Hsp104 and of NBD
mutants. In physiological ionic strength buffers (pH 7.5, 37° C) WT Hsp104 exhibits
Michaelis-Menten kinetics between 0.5 and 25 mm ATP (K m∼ 5 mm, V max∼ 2 nmol min−
1 μg− 1). ATPase activity is strongly influenced by factors that vary with cell stress (eg …
