© 2005 The Japanese Biochemical Society
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Constantly Updated Knowledge of Hsp90
1 Department of Biophysics and Biochemistry and 2 Undergraduate Program for Bioinformatics and Systems Biology, Graduate School of Science, The University of Tokyo, Hongo 7-3-1, Bunkyo-ku, Tokyo 113-0033; 3 Department of Natural and Environmental Science, Faculty of Education, Tokyo Gakugei University, Nukuikitamachi 4-1-1, Koganei, Tokyo 184-8501; and 4 Department of Biochemistry and Molecular Biology, Faculty of Medicine, The University of Tokyo, Hongo 7-3-1, Bunkyo-ku, Tokyo 113-0033
* To whom correspondence should be addressed. Tel/Fax: +81-3-5841-3047, E-mail: yminami{at}biochem.s.u-tokyo.ac.jp
Although protein folding, in principle is a spontaneous process which depends only upon the amino-acid sequence, the assistance of molecular chaperones is required for many proteins to achieve their final conformation in vivo. While Hsp90 is one of the major molecular chaperones, it has long been the most mysterious among them. Recent advances in our knowledge regarding Hsp90 structure and function, owing to both detailed biochemical and genetic characterizations of Hsp90 co-chaperones, as well as eminent structural studies have established Hsp90 as an ATPase-dependent chaperone, and have provided a paradigm of the Hsp90 chaperone cycle, which is sequentially tuned and coordinated by a variety of co-chaperones. Here we summarize the current knowledge regarding the structure and essential activities of Hsp90, which certainly promises a deeper understanding of the functions of Hsp90 in vivo.
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