Paf1 and Ctr9 subcomplex formation is essential for Paf1 complex assembly and functional regulation

Ying Xie, Minying Zheng, Xinlei Chu, Yue Chen, Huisha Xu, Jiawei Wang, Hao Zhou () and Jiafu Long ()
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Ying Xie: Nankai University
Minying Zheng: Nankai University
Xinlei Chu: Tianjin Medical University Cancer Institute and Hospital
Yue Chen: Nankai University
Huisha Xu: Nankai University
Jiawei Wang: Tsinghua University
Hao Zhou: Nankai University
Jiafu Long: Nankai University

Nature Communications, 2018, vol. 9, issue 1, 1-13

Abstract: Abstract 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.

Date: 2018
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DOI: 10.1038/s41467-018-06237-7

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