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. Author manuscript; available in PMC: 2018 Jul 15.
Published in final edited form as: Cancer Res. 2018 Jan 8;78(2):313–319. doi: 10.1158/0008-5472.CAN-17-2175

Figure 1. PAF1 complex (PAF1C) and its interacting partners.

Figure 1

Human PAF1C consists of 5 components: PAF1 or PD2 (Pancreatic differentiation 2), CDC73, SKI8, LEO1, and CTR9. The domain organization of PD2/PAF1 consists of three Myc type helix-loop-helix, a leucine zipper (LZ), an RNA recognition motif (RRM), Ser/Asp-rich region, a Glu-rich domain and a nuclear localization signal (NLS). PAF1C interacts with a variety of factors involved in histone covalent modifications, transcription and mRNA 3′ end processing. These include histone chaperone FACT (Facilitates chromatin transcription), RNF20/RNF40 (that catalyzes histone H2B monoubiquitination), methyltransferases such as mixed lineage leukemia 1 (MLL1) that methylates histone H3 at K4, RNA Pol II, CDK12/Cyclin K complex, positive transcription elongation factor b (P-TEFb), elongation factors such as TFIIS (Dst1/SII) and DRB sensitivity-inducing factor (DSIF), human cleavage and poly (A) factors that include cleavage and polyadenylation specificity factor (CPSF) and cleavage stimulation factor (CstF).