2000年5月
Divergent hTAF(II)31-binding motifs hidden in activation domains
JOURNAL OF BIOLOGICAL CHEMISTRY
- ,
- ,
- 巻
- 275
- 号
- 21
- 開始ページ
- 15912
- 終了ページ
- 15916
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1074/jbc.275.21.15912
- 出版者・発行元
- AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Activation domains are functional modules that enable DNA-binding proteins to stimulate transcription. Characterization of these essential modules in transcription factors has been hampered by their low sequence homology. Here we delineate the peptide sequences that are required for transactivation and interaction with hTAF(II)31, a classical target of the acidic class of activation domains. Our analyses indicate that hTAF(II)31 recognizes a diverse set of sequences for transactivation. This information enabled the identification of hTAF(II) 31-binding sequences that are critical for the activity of the activation domains of five human transcription factors: NFAT1, ALL1, NF-IL6, ESX, and HSF-1. The interaction surfaces are localized in short peptide segments of activation domains. The brevity and heterogeneity of the motifs may explain the low sequence homology among acidic activation domains.
- リンク情報
- ID情報
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- DOI : 10.1074/jbc.275.21.15912
- ISSN : 0021-9258
- Web of Science ID : WOS:000087291400042