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Divergent hTAFII31-binding motifs hidden in activation domains.

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.

Pubmed ID: 10821850


  • Choi Y
  • Asada S
  • Uesugi M


The Journal of biological chemistry

Publication Data

May 26, 2000

Associated Grants


Mesh Terms

  • Amino Acid Sequence
  • Binding Sites
  • Gene Expression Regulation
  • Humans
  • Jurkat Cells
  • Magnetic Resonance Spectroscopy
  • Molecular Sequence Data
  • Mutation
  • NFATC Transcription Factors
  • Peptide Fragments
  • Peptide Library
  • Protein Binding
  • Sequence Alignment
  • TATA-Binding Protein Associated Factors
  • Trans-Activators
  • Transcription Factor TFIID
  • Transcription Factors
  • Transcription, Genetic
  • Transcriptional Activation