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Significance The highly conserved polymerase-associated factor 1 complex (PAF1C) is composed of five core subunits (Ctr9, Paf1, Cdc73, Rtf1, and Leo1) and involved in all stages of RNA polymerase II… Click to show full abstract
Significance The highly conserved polymerase-associated factor 1 complex (PAF1C) is composed of five core subunits (Ctr9, Paf1, Cdc73, Rtf1, and Leo1) and involved in all stages of RNA polymerase II (RNAPII)-mediated transcription. This study involves biochemical and mechanistic insights into the role of PAF1C subunits in regulating the RNAPII pool in response to DNA damage via a previously uncharacterized multistep pathway. The data from both in vivo and in vitro assays clearly revealed that PAF1C orchestrates the exchange of Spt5 and Rad26 via the Rtf1 subunit and the recruitment of the Elongin-Cullin E3 complex to stalled RNAPII via the heterodimer Paf1/Leo1 in concert with Rad26, thereby facilitating RNAPII removal.
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Year Published: 2022
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