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

By K. Kinkelin, Glenn G. Wozniak, Scott B. Rothbart, Michael Lidschreiber, Brian D. Strahl, Patrick Cramer. 2013

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DIDO as a Switchboard that Regulates Self-Renewal and Differentiation in Embryonic Stem Cells (2017, methodology): “We found that DIDO3 binds RNA POL II and thus links DIDO to transcriptional control, as shown for the yeast DIDO homolog BYE1 (Kinkelin et al., 2013; Pinskaya et al., 2014).”
Interplay between splicing and transcriptional pausing exerts genome-wide control over alternative polyadenylation (2021, background): “The protein family also binds to the jaw and funnel domains of RNA Pol II [21], leading to a bivalent genomic distribution at both gene ends [24,25].”
A Unique pH-Dependent Recognition of Methylated Histone H3K4 by PPS and DIDO. (2017, background): “, 2013) and Bye1 directly associating with the RNA polymerase II in yeast (Kinkelin et al., 2013; Pinskaya et al., 2014).”
Dido3-dependent SFPQ recruitment maintains efficiency in mammalian alternative splicing (2019, background): “Dido3 is probably bound to RNA pol II via its TFIIS domain (25,30), which indicates that the two move together during RNA synthesis (26,30).”