| Autor: |
Kotani, Tomohiro, Miyake, Tsuyoshi, Tsukihashi, Yoshihiro, Hinnebusch, Alan G., Nakatani, Yoshihiro, Kawaichi, Masashi, Kokubo, Tetsuro |
| Zdroj: |
Journal of Biological Chemistry; November 1998, Vol. 273 Issue: 48 p32254-32264, 11p |
| Abstrakt: |
TFIID is a multiprotein complex composed of TBP and several TAFIIs. Small amino-terminal segments (TAF N-terminal domain (TAND)) of DrosophilaTAFII230 (dTAFII230) and yeast TAFII145 (yTAFII145) bind strongly to TBP and inhibit TBP-DNA interactions. yTAFII145 TAND (yTAND) was divided into two subdomains, yTANDI10–37and yTANDII46–71, that function cooperatively. Here, we identify dTANDII within the amino terminus of dTAFII230 at 118–143 amino acids in addition to dTANDI18–77, reported previously. dTANDII exhibits pronounced sequence similarity to yTANDII, and the two were shown to be functionally equivalent in binding to TBP and inhibiting TBP-DNA interactions in vitro. Alanine scanning mutation analysis demonstrated that Phe-57 (yTANDII) and Tyr-129 (dTANDII) are critically required for the interaction with TBP. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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