Scheibel, Thomas and Neuhofen, Sonja and Weikl, Tina and Mayr, Christian and Reinstein, Jochen and Vogel, Pia D. and Buchner, Johannes (1997) ATP-binding properties of human Hsp90. JOURNAL OF BIOLOGICAL CHEMISTRY, 272 (30). pp. 18608-18613. ISSN 0021-9258, 1083-351X
Full text not available from this repository.Abstract
Hsp90 is one of the most abundant proteins in the cytosol of eukaryotic cells, Under physiological conditions Hsp90 has been shown to play a major role in several specific signaling pathways, including maturation of various kinases and maintenance of steroid receptors in an activable state. It is well established that the level of Hsp90 increases severalfold under stress conditions, and it has been shown that the chaperone function of Hsp90 is ATP-independent. Although yeast Hsp90 does not bind ATP, as determined by a number of methods monitoring tight binding, ATP dependent functions of Hsp90 in the presence of co-factors and elevated temperatures are still under discussion. Here, we have reinvestigated ATP-binding properties and ATPase activity of human Hsp90 under various conditions, We show that human Hsp90 does not bind ATP tightly and does not exhibit detectable ATPase activity. However, using electron spin resonance spectroscopy, weak binding of spin-labeled ATP analogues with half-maximal binding at 400 mu M ATP was detected. The functional significance of this weak interaction remains enigmatic.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | HEAT-SHOCK PROTEINS; GLUCOCORTICOID RECEPTOR INACTIVATION; SPIN-RESONANCE SPECTROSCOPY; PROGESTERONE-RECEPTOR; MOLYBDATE IONS; KINASE; EPIMERIZATION; CHAPERONES; ACTIVATION; MECHANISM |
| Subjects: | 500 Science > 540 Chemistry & allied sciences 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 25 Apr 2023 08:56 |
| Last Modified: | 25 Apr 2023 08:56 |
| URI: | https://pred.uni-regensburg.de/id/eprint/50693 |
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