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.
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
Mol. Cell
Date: Apr. 23, 2004
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