Volume 10 Issue 11, November 2003

The new crystal structure of the IRF-3 transactivation domain reveals an evolutionarily conserved protein domain whose activity is modulated by phosphorylation controlling oligomerization and protein-protein interactions.

Two recent reports show that the rate of transcription elongation affects splice site selection and exon skipping and, thereby, the nature of the information expressed from a gene.

Recent studies suggest that the Spt16 protein of FACT shuttles H2A–H2B dimers off and on nucleosomes during transcription elongation. By restoring nucleosomes after passage of RNA polymerase II, Spt16 and Spt6 prevent transcription from cryptic promoters in coding regions that would otherwise be expressed in the absence of histones.