[HTML][HTML] The importance of ATP binding and hydrolysis by hsp90 in formation and function of protein heterocomplexes
JP Grenert, BD Johnson, DO Toft - Journal of Biological Chemistry, 1999 - ASBMB
The chaperone hsp90 is capable of binding and hydrolyzing ATP. Using information on a
related ATPase, DNA gyrase B, we selected three conserved residues in hsp90's ATP-
binding domain for mutation. Two of these mutations eliminate nucleotide binding, while the
third retains nucleotide binding but is apparently deficient in ATP hydrolysis. We first
analyzed how these mutations affect hsp90's binding to the co-chaperones p23 and Hop,
and to the hydrophobic resin, phenyl-Sepharose. These experiments showed that ATP's …
related ATPase, DNA gyrase B, we selected three conserved residues in hsp90's ATP-
binding domain for mutation. Two of these mutations eliminate nucleotide binding, while the
third retains nucleotide binding but is apparently deficient in ATP hydrolysis. We first
analyzed how these mutations affect hsp90's binding to the co-chaperones p23 and Hop,
and to the hydrophobic resin, phenyl-Sepharose. These experiments showed that ATP's …