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Gene-specific modulation of TAF10 function by SET9-mediated methylation.

SET9 is a member of the SET domain-containing histone methyltransferase family that can specifically methylate histone 3 at lysine 4 position. Although nucleosomal histones are poor substrates for SET9, the active enzyme can stimulate activator-induced transcription. Here, we show that SET9 can monomethylate the TBP-associated factor TAF10 at a single lysine residue located at the loop 2 region within the putative histone-fold domain of the protein. Methylated TAF10 has an increased affinity for RNA polymerase II, pointing to a direct role of this modification in preinitiation complex formation. Reporter assays and studies on TAF10 null F9 cells expressing a methylation-deficient TAF10 mutant revealed that SET9-mediated methylation of TAF10 potentiates transcription of some but not all TAF10-dependent genes. This gene specificity correlated with SET9 recruitment. The promoter-specific effects of SET9-methylated TAF10 may have important implications regarding the biological function of SET domain-containing lysine methylases, whose primary targets have been presumed to be histones.

Pubmed ID: 15099517


  • Kouskouti A
  • Scheer E
  • Staub A
  • Tora L
  • Talianidis I


Molecular cell

Publication Data

April 23, 2004

Associated Grants


Mesh Terms

  • Amino Acid Sequence
  • Antibodies, Monoclonal
  • Baculoviridae
  • Binding Sites
  • Cell Line
  • Cell Nucleus
  • Escherichia coli
  • Gene Expression Regulation
  • Genes, Reporter
  • Genetic Vectors
  • HeLa Cells
  • Histones
  • Humans
  • Lysine
  • Methylation
  • Methyltransferases
  • Mutation
  • Nucleosomes
  • Precipitin Tests
  • Protein Structure, Tertiary
  • Proteins
  • RNA Polymerase II
  • Recombinant Fusion Proteins
  • Substrate Specificity
  • TATA-Binding Protein Associated Factors
  • Time Factors
  • Transcription Factor TFIID
  • Transcription, Genetic
  • Transcriptional Activation