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Ubiquitin-activating/conjugating activity of TAFII250, a mediator of activation of gene expression in Drosophila.

Ubiquitination of histones has been linked to the complex processes that regulate the activation of eukaryotic transcription. However, the cellular factors that interpose this histone modification during the processes of transcriptional activation are not well characterized. A biochemical approach identified the Drosophila coactivator TAFII250, the central subunit within the general transcription factor TFIID, as a histone-specific ubiquitin-activating/conjugating enzyme (ubac). TAFII250 mediates monoubiquitination of histone H1 in vitro. Point mutations within the putative ubac domain of TAFII250 abolished H1-specific ubiquitination in vitro. In the Drosophila embryo, inactivation of the TAFII250 ubac activity reduces the cellular level of monoubiquitinated histone H1 and the expression of genes targeted by the maternal activator Dorsal. Thus, coactivator-mediated ubiquitination of proteins within the transactivation pathway may contribute to the processes directing activation of eukaryotic transcription.

Pubmed ID: 11009423

Authors

  • Pham AD
  • Sauer F

Journal

Science (New York, N.Y.)

Publication Data

September 29, 2000

Associated Grants

None

Mesh Terms

  • Acetyltransferases
  • Animals
  • DNA-Binding Proteins
  • Drosophila
  • Drosophila Proteins
  • Embryo, Nonmammalian
  • Gene Expression Regulation
  • Histone Acetyltransferases
  • Histones
  • In Situ Hybridization
  • Ligases
  • Mutation
  • Nuclear Proteins
  • Phosphoproteins
  • Point Mutation
  • Protein Structure, Tertiary
  • Recombinant Proteins
  • Saccharomyces cerevisiae Proteins
  • TATA Box
  • TATA-Binding Protein Associated Factors
  • Trans-Activators
  • Transcription Factor TFIID
  • Transcription Factors
  • Transcription Factors, TFII
  • Transcriptional Activation
  • Ubiquitin-Activating Enzymes
  • Ubiquitin-Conjugating Enzymes
  • Ubiquitin-Protein Ligases
  • Ubiquitins