Paf1 and Ctr9 subcomplex formation is essential for Paf1 complex assembly and functional regulation.
The evolutionarily conserved multifunctional polymerase-associated factor 1 (Paf1) complex (Paf1C), which is composed of at least five subunits (Paf1, Leo1, Ctr9, Cdc73, and Rtf1), plays vital roles in gene regulation and has connections to development and human diseases. Here, we report two structures of each of the human and yeast ... Ctr9/Paf1 subcomplexes, which assemble into heterodimers with very similar conformations, revealing an interface between the tetratricopeptide repeat module in Ctr9 and Paf1. The structure of the Ctr9/Paf1 subcomplex may provide mechanistic explanations for disease-associated mutations in human PAF1 and CTR9. Our study reveals that the formation of the Ctr9/Paf1 heterodimer is required for the assembly of yeast Paf1C, and is essential for yeast viability. In addition, disruption of the interaction between Paf1 and Ctr9 greatly affects the level of histone H3 methylation in vivo. Collectively, our results shed light on Paf1C assembly and functional regulation.
Mesh Terms:
Cell Cycle Proteins, Cell Survival, Crystallography, X-Ray, DNA Methylation, Gene Expression Regulation, HEK293 Cells, Histones, Humans, Nuclear Proteins, Phosphoproteins, Protein Multimerization, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Transcriptional Elongation Factors
Cell Cycle Proteins, Cell Survival, Crystallography, X-Ray, DNA Methylation, Gene Expression Regulation, HEK293 Cells, Histones, Humans, Nuclear Proteins, Phosphoproteins, Protein Multimerization, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Transcriptional Elongation Factors
Nat Commun
Date: Dec. 18, 2017
PubMed ID: 30228257
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