1998 Fiscal Year Final Research Report Summary
Transcriptional activation domain of p300/CBP-associated factor(P/CAF)
| Project/Area Number |
09672226
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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 |
Biological pharmacy
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| Research Institution | Osaka University |
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Principal Investigator |
NISHIKAWA Jun-ichi Graduate School of Pharmaceutical Sciences ; Research Associate, 薬学研究科, 助手 (90218131)
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| Project Period (FY) |
1997 – 1998
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| Keywords | transcriptional regulation / histone acetyltransferase / chromatin |
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| Research Abstract |
In eukaryores, transcription of mRNA-encoding classII genes involves the ordered recruitment of general factors and the RNA polymerase II holoenzyme into the basal transcription pre-initiation complex on promoter.The transcription is efficiently enhanced by transcriptional activators which bind to specific DNA sequences outside of the core promoter.Sequence-specific activators work in conjunction with other factors which do not bind DNA directly.These factors are termed co-activators and are recruited to promoters via their interaction with the DNA-bound transcription factors.P/CAF was originally identified as a p300/CBP-binding protein by virtue of its sequence similarity to a yeast histone acetyltransferase (HAT), namely yGCN5.In addition, P/CAF interacts with other co-activators such as ACIR and SRC-1 which are also HAT.In this study, I focused on the function of P/CAF in the transcriptional regulation and investigated the transcriptional activation domain of P/CAF.
In order to examine the activation function of P/CAF, I expressed various regions of P/CAF as GALA DNA binding domain in yeast.P/CAF indeed worked as a transcriptional activator protein in yeast and the region of amino acids 366-654 was necessary for activation function.As this region is identical to the HAT domain, the activation function of P/CAF might be related to the acetylation of histones.On the other hand, the interaction of P/CAF with CBP was independent on the activation domain. The complex formation of co-activators in vitro was also examined using surface plasmon resonance anaysis.
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