7DKH

Crystal structure of the Ctr9/Paf1/Cdc73/Rtf1 quaternary complex

Summary for 7DKH

• Entry DOI: 10.2210/pdb7dkh/pdb
• Descriptor: RNA polymerase-associated protein CTR9, RNA polymerase II-associated protein 1, Cell division control protein 73, ... (4 entities in total)
• Functional Keywords: paf1 complex, h2b mono-ubiquitination, rad6/bre1, ubiquitin discharge, gene regulation
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Total number of polymer chains: 12
• Total formula weight: 420730.42

Authors

Chen, F.L.,Liu, B.B.,Guo, L.,Li, D.F.,Zhou, H.,Long, J.F. (deposition date: 2020-11-24, release date: 2021-11-24, Last modification date: 2024-11-13)

Primary citation

Chen, F.L.,Liu, B.B.,Zeng, J.W.,Guo, L.,Ge, X.,Feng, W.,Li, D.F.,Zhou, H.,Long, J.F.
Crystal Structure of the Core Module of the Yeast Paf1 Complex.
J.Mol.Biol., 434:167369-167369, 2021

PubMed Abstract: The highly conserved multifunctional polymerase-associated factor 1 (Paf1) complex (PAF1C), which consists of five core subunits: Ctr9, Paf1, Leo1, Cdc73, and Rtf1, acts as a diverse hub that regulates all stages of RNA polymerase II-mediated transcription and various other cellular functions. However, the underlying mechanisms remain unclear. Here, we report the crystal structure of the core module derived from a quaternary Ctr9/Paf1/Cdc73/Rtf1 complex of S. cerevisiae PAF1C, which reveals interfaces between the tetratricopeptide repeat module in Ctr9 and Cdc73 or Rtf1, and find that the Ctr9/Paf1 subcomplex is the key scaffold for PAF1C assembly. Our study demonstrates that Cdc73 binds Ctr9/Paf1 subcomplex with a very similar conformation within thermophilic fungi or human PAF1C, and that the binding of Cdc73 to PAF1C is important for yeast growth. Importantly, our structure reveals for the first time that the extreme C-terminus of Rtf1 adopts an "L"-shaped structure, which interacts with Ctr9 specifically. In addition, disruption of the binding of either Cdc73 or Rtf1 to PAF1C greatly affects the normal level of histone H2B K123 monoubiquitination in vivo. Collectively, our results provide a structural insight into the architecture of the quaternary Ctr9/Paf1/Cdc73/Rtf1 complex and PAF1C functional regulation.

PubMed: 34852272
DOI: 10.1016/j.jmb.2021.167369

Experimental method

X-RAY DIFFRACTION (2.9 Å)