ヨゴサワ　シンゴ   YOGOSAWA Shingo   与五沢　真吾    所属   埼玉医科大学  保健医療学部 臨床検査学科    職種   准教授
論文種別	学術雑誌(原著)
言語種別	英語
査読の有無	査読あり
表題	Multiple mammalian proteasomal ATPases, but not proteasome itself, are associated with TATA-binding protein and a novel transcriptional activator, TIP120
掲載誌名	正式名：GENES TO CELLS ISSNコード：1356-9597
出版社	BLACKWELL SCIENCE LTD
巻・号・頁	4(9),529-539頁
著者・共著者	Y Makino,T Yoshida,S Yogosawa,K Tanaka,M Muramatsu,T Tamura
発行年月	1999/09
概要	Background: SUG1 belongs to proteasomal ATPase, Previous studies have demonstrated that SUG1 is associated with TBP. It is assumed to be involved in transcriptional regulation in addition to proteolysis, In this study, we investigated the association of mammalian SUG1 with TBP in more detail. Results: Pull-down experiments with TBP revealed multiple TBP-interacting proteins (TIPs) that were recovered dependent upon the presence of C-terminal conserved domain of TBP. By 2-D electrophoresis, we identified SUG1 in TIPs, By using far-Western analysis, we identified two proteins that could directly bind to TBP: SUG1 and another proteasomal ATPase (S4). Protein microsequencing and Western blotting identified all the remaining proteasomal ATPases (MSS1, TBP1, TBP7, and SUG2) in the TIP preparations. We present evidence that TBP and at least SUGI, MSS1, and S4 form a complex in the cell. However, no evidence of association of TBP with the 26S proteasome or its 19S regulatory unit was obtained. The molecular mass of the TBP/ATPases-complex, which also included a novel transcription regulatory factor, TTP120, was estimated to be approximate to 800 kDa. Conclusion: These results suggest that there is a novel multisubunit complex containing TBP and proteasomal ATPases, Based on our findings, we hypothesize that proteasomal ATPases are involved in transcriptional regulation in addition to proteolysis.
DOI	10.1046/j.1365-2443.1999.00277.x
NAID	80010748262
PMID	10526239