Subunit Interactions Influence the Biochemical and Biological Properties of Hsp104

Point mutations in either of the two nucleotide-binding domains (NBD) of Hsp104 (NBD1 and NBD2) eliminate its thermotolerance function in vivo. In vitro, NBD1 mutations virtually eliminate ATP hydrolysis with little effect on hexamerization; analogous NBD2 mutations reduce ATPase activity and severe...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2001-01, Vol.98 (3), p.914-919
Hauptverfasser:	Schirmer, Eric C., Ware, Danielle M., Queitsch, Christine, Kowal, Anthony S., Lindquist, Susan L.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine triphosphatases Adenosine Triphosphatases - chemistry Adenosine Triphosphatases - metabolism Adenosine Triphosphate - metabolism Amino Acid Substitution Binding Sites Biological Sciences Coefficients Computer software Cooperation Estradiol - pharmacology Fungal Proteins - chemistry Fungal Proteins - metabolism Heat tolerance Heat-Shock Proteins - chemistry Heat-Shock Proteins - metabolism Hsp104 protein Hydrolysis Kinetics Mutagenesis, Site-Directed Oligomers Phosphates Point Mutation Protein Subunits Proteins Recombinant Proteins - chemistry Recombinant Proteins - metabolism Saccharomyces cerevisiae - drug effects Saccharomyces cerevisiae - growth & development Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins
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