Structural and enzymatic properties of the AAA protein Drg1p from Saccharomyces cerevisiae. Decoupling of intracellular function from ATPase activity and hexamerization

The AAA protein Drg1 from yeast was affinity-purified, and its ATPase activity and hexamerization properties were analyzed. The same parameters were also determined for several mutant proteins and compared in light of the growth characteristics of the corresponding cells. The protein from a thermose...

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Veröffentlicht in:	The Journal of biological chemistry 2002-07, Vol.277 (30), p.26788-26795
Hauptverfasser:	Zakalskiy, Andriy, Högenauer, Gregor, Ishikawa, Takashi, Wehrschütz-Sigl, Eva, Wendler, Franz, Teis, David, Zisser, Gertrude, Steven, Alasdair C, Bergler, Helmut
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphatases - chemistry Adenosine Triphosphatases - genetics Adenosine Triphosphatases - metabolism Adenosine Triphosphate - metabolism Alleles Binding Sites Boron Compounds - pharmacology Centrifugation, Density Gradient Cloning, Molecular Fungal Proteins - biosynthesis Fungal Proteins - chemistry Glycerol - pharmacology Kinetics Microscopy, Electron Mutation Protein Binding Protein Structure, Tertiary Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Temperature
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