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| Subject Categories: Proteins |
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| The EMBO Journal
(2003) 22, 3557–3567, doi:10.1093/emboj/cdg349 |
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| The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasome |
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| Jun Imai1, 2, 3, Mikako Maruya2, 3, Hideki Yashiroda1, 3, Ichiro Yahara3, 4 and Keiji Tanaka1, 3 |
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1 Department of Molecular Oncology, Tokyo Metropolitan Institute of Medical Science, Honkomagome 3-18-22, Bunkyo-ku, Tokyo 113-8613, Japan 2 Department of Cell Biology, Tokyo Metropolitan Institute of Medical Science, Honkomagome 3-18-22, Bunkyo-ku, Tokyo 113-8613, Japan 3 CREST, Japan Science and Technology Corporation, Honmachi 4-1-8, Kawaguchi, Saitama 332-0012, Japan 4 Ina Laboratory, Medical and Biological Laboratories Co. Ltd, 1063-103 Ohara Terasawaoka, Ina, Nagano 396-0002, Japan To whom correspondence should be addressed Keiji Tanaka, tanakak@rinshoken.or.jp Received 20 January 2003; Revised 20 May 2003; Accepted 21 May 2003. |
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| Abstract |
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| Hsp90 has a diverse array of cellular roles including protein folding, stress response and signal transduction. Herein we report a novel function for Hsp90 in the ATP-dependent assembly of the 26S proteasome. Functional loss of Hsp90 using a temperature-sensitive mutant in yeast caused dissociation of the 26S proteasome. Conversely, these dissociated constituents reassembled in Hsp90-dependent fashion both in vivo and in vitro; the process required ATP-hydrolysis and was suppressed by the Hsp90 inhibitor geldanamycin. We also found genetic interactions between Hsp90 and several proteasomal Rpn (Regulatory particle non-ATPase subunit) genes, emphasizing the importance of Hsp90 to the integrity of the 26S proteasome. Our results indicate that Hsp90 interacts with the 26S proteasome and plays a principal role in the assembly and maintenance of the 26S proteasome. |
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| Keywords: assembly, Hsp90, maintenance, 26S proteasome, yeast |
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