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Significance The polymerase associated factor 1 complex (Paf1C) is an RNA polymerase (pol) II accessory factor that broadly influences gene expression by regulating chromatin structure and the recruitment of RNA-processing factors during transcription. This study shows how phosphorylation of a repeated motif within an additional factor, Spt5, is recognized and used by the Plus3 domain within the Paf1C subunit Rtf1 (restores TBP function 1) to promote recruitment of Paf1C to the transcription machinery. Deletions of both the Rtf1 Plus3 domain and the C domain of Cdc73 (Cell Division Cycle 73) are required to abolish Paf1C-mediated histone modifications and chromatin occupancy suggesting that dual attachment points facilitate the association of Paf1C with RNA pol II.

Structural basis for Spt5-mediated recruitment of the Paf1 complex to chromatin