1998 Fiscal Year Final Research Report Summary
Functional analysis of TAND (TAF N-terminal domain) that inhibits TBP : DNA interactions
| Project/Area Number |
09680677
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Molecular biology
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| Research Institution | Nara Institute of Science and Technology |
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Principal Investigator |
KOKUBO Tetsuro Nara Institute of Science and Technology, Graduate School of Biological Sciences, Associate Professor, バイオサイエンス研究科, 助教授 (10271587)
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| Co-Investigator(Kenkyū-buntansha) |
KASAHARA Kouji Nara Institute of Science and Technology, Graduate School of Biological Sciences, バイオサイエンス研究科, 助手 (40304159)
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| Project Period (FY) |
1997 – 1998
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| Keywords | transcription / TFIID / general transcription factor / TAF / TAND / activation / transcriptional regulation |
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| Research Abstract |
TFIID is a multiprotein complex comprised of TBP and several TAFlls. Small N-terminal segments (TAND ; TAF N-terminal Domain) of Drosophila TAFll23O (dTAFll230) and yeast TAFll145 (yTAFll145) bind strongly to TBP and thereby inhibit TBP : DNA interactions. dTAFll230 TAND (dTAND) and yTAFll145 TAND (yTAND) were further divided into two subdomains, dTANDI (18-77 aa) & II(118-143 aa), and yTANDI (10-37 aa) & II(46-71 aa), respectively, that function cooperatively. More importantly, TANDI and TANDII compete with activators and TFIIA, respectively, for TBP binding. We also demonstrated the functional conservation between activation domains and TANDI.When fused to the DNA-binding domain, TANDI functions as an activation domain in yeast. Conversely, activation domains function as TANDI when TANDI is replaced with activation domains within TEIID.Furthermore, we show that the interaction with the concave surface of TBP is crucial for the functions of both activators and TAN DI.These results indicate that transcriptional activation steps include suppression of the inhibitory activity of TANDI by transcriptional activators.
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