Structures of RNA polymerase II complexes with Bye1, a chromatin-binding PHF3/DIDO homologue

摘要: Bypass of Ess1 (Bye1) is a nuclear protein with domain resembling the central in transcription elongation factor TFIIS. Here we show that Bye1 binds its TFIIS-like (TLD) to RNA polymerase (Pol) II, and report crystal structures TLD bound Pol II three different II–nucleic acid complexes. Like TFIIS, jaw funnel. In contrast however, it neither alters conformation nor vitro functions II. vivo, recruited chromatin via occupies 5′-region active genes. A plant homeo (PHD) histone H3 tails trimethylated lysine 4, this interaction enhanced by presence neighboring posttranslational modifications (PTMs) mark conversely impaired repressive PTMs. We identify putative human homologs Bye1, proteins PHD finger 3 death-inducer obliterator, which are both implicated cancer. These results establish as founding member unique family factors link histones PTMs transcribing