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Structure of the Yeast Ctr9/Paf1 complex
Structural highlights
Function[CTR9_YEAST] The PAF1 complex is a multifunctional complex. Involved in transcription initiation via genetic interactions with TATA-binding proteins. Involved in elongation. It regulates 3'-end formation of snR47 by modulating the recruitment or stable association of NRD1 and NAB3 with RNA polymerase II. Also has a role in transcription-coupled histone modification. Required for activation of RAD6 ubiquitin conjugate and the BRE1 ubiquitin ligase which ubiquitinate 'Lys-126' histone H2B. Activates the SET1 histone methyltransferase complex for methylation of 'Lys-4' of histone H3 and for methylation of 'Lys-73' of histone H3 by DOT1 and 'Lys-36' of histone H3 by SET2. In complex with PAF1, required for normal CLN1 and CLN2 G1 cyclin expression in late G1. Also has a role in chromosome segregation where it appears to be involved in microtubule placement.[1] [2] [3] [4] Publication Abstract from PubMedThe 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. Paf1 and Ctr9 subcomplex formation is essential for Paf1 complex assembly and functional regulation.,Xie Y, Zheng M, Chu X, Chen Y, Xu H, Wang J, Zhou H, Long J Nat Commun. 2018 Sep 18;9(1):3795. doi: 10.1038/s41467-018-06237-7. PMID:30228257[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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